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}.
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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
//