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Database: UniProt
Entry: G8YH79_PICSO
LinkDB: G8YH79_PICSO
Original site: G8YH79_PICSO 
ID   G8YH79_PICSO            Unreviewed;       154 AA.
AC   G8YH79;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   10-APR-2019, entry version 35.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=Piso0_003112 {ECO:0000313|EMBL:CCE80781.1};
GN   ORFNames=GNLVRS01_PISO0G05154g {ECO:0000313|EMBL:CCE80016.1},
GN   GNLVRS01_PISO0H05155g {ECO:0000313|EMBL:CCE80781.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 /
OS   NBRC 10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE80781.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|EMBL:CCE80781.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M.,
RA   Mallet S., Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J.,
RA   Seret M.L., Talla E., Samson G., Jubin C., Poulain J., Vacherie B.,
RA   Barbe V., Pelletier E., Sherman D.J., Westhof E., Weissenbach J.,
RA   Baret P.V., Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps
RT   of genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(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:
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; FO082053; CCE80016.1; -; Genomic_DNA.
DR   EMBL; FO082052; CCE80781.1; -; Genomic_DNA.
DR   STRING; 4920.XP_004201153.1; -.
DR   EnsemblFungi; CCE80016; CCE80016; GNLVRS01_PISO0G05154g.
DR   EnsemblFungi; CCE80781; CCE80781; GNLVRS01_PISO0H05155g.
DR   Proteomes; UP000005222; Chromosome H.
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   PRINTS; PR00068; CUZNDISMTASE.
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:UP000005222};
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:UP000005222};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15957 MW;  6CF05C3115DB9341 CRC64;
     MVKAVAVLRG DSKVNGVVHF EQNSESEPTT VSWEIEGNDA NALRGFHIHQ FGDNTNGCTS
     AGPHFNPFSK EHGAPEDDNR HVGDLGNITT DASGVAKGTK QDLLIKLLGA NSILGRTVVV
     HSGTDDLGKG GNAESKKTGN AGTRPACGVI GIGN
//
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