GenomeNet

Database: UniProt
Entry: Q70CE4_FAGSY
LinkDB: Q70CE4_FAGSY
Original site: Q70CE4_FAGSY 
ID   Q70CE4_FAGSY            Unreviewed;       166 AA.
AC   Q70CE4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
DE   Flags: Fragment;
GN   Name=sod1 {ECO:0000313|EMBL:CAE54085.1};
OS   Fagus sylvatica (Beechnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Fagaceae; Fagus.
OX   NCBI_TaxID=28930 {ECO:0000313|EMBL:CAE54085.1};
RN   [1] {ECO:0000313|EMBL:CAE54085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seed {ECO:0000313|EMBL:CAE54085.1};
RA   Jimenez-Nieto J.A.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAE54085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seed {ECO:0000313|EMBL:CAE54085.1};
RA   Jimenez Nieto J.A.;
RT   "Aislamiento y caracterizacion de clones de cDNA en semillas durmientes de
RT   Fagus sylvatica.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001605};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ586519; CAE54085.1; -; mRNA.
DR   AlphaFoldDB; Q70CE4; -.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAE54085.1}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          29..162
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAE54085.1"
SQ   SEQUENCE   166 AA;  16725 MW;  EB08EAC88AD85637 CRC64;
     SVPTARGVLR SHRTMAKGVA VLSSNEGVCG TIYFAQEGDG PTTVTGNISG LKPGLHGFHV
     HALGDTTNGC MSTGPHFNPA GKEHGAPEDA NRHAGDLGNV NVGDDGTVSF TIIDKQIPLC
     GPNSIIGRAV VVHGDPDDLG KGGHELSKST GNAGGRIACG IIGLQG
//
DBGET integrated database retrieval system