ID SODC2_MAIZE Reviewed; 151 AA.
AC P11428;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 2;
DE EC=1.15.1.1;
GN Name=SODCC.1; Synonyms=SOD2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3467349; DOI=10.1073/pnas.84.1.179;
RA Cannon R.E., White J.A., Scandalios J.G.;
RT "Cloning of cDNA for maize superoxide dismutase 2 (SOD2).";
RL Proc. Natl. Acad. Sci. U.S.A. 84:179-183(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3597043;
RA Cannon R.E., Scandalios J.G.;
RT "The superoxide dismutase-2 gene of maize.";
RL Isozymes Curr. Top. Biol. Med. Res. 14:73-81(1987).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M15175; AAA33511.1; -; mRNA.
DR EMBL; M54936; AAA33510.1; -; mRNA.
DR PIR; A29077; A29077.
DR RefSeq; NP_001105335.1; NM_001111865.1.
DR RefSeq; XP_008651856.1; XM_008653634.1.
DR AlphaFoldDB; P11428; -.
DR SMR; P11428; -.
DR STRING; 4577.P11428; -.
DR PaxDb; 4577-GRMZM2G025992_P01; -.
DR EnsemblPlants; Zm00001eb330020_T001; Zm00001eb330020_P001; Zm00001eb330020.
DR EnsemblPlants; Zm00001eb330020_T004; Zm00001eb330020_P004; Zm00001eb330020.
DR EnsemblPlants; Zm00001eb330020_T006; Zm00001eb330020_P006; Zm00001eb330020.
DR GeneID; 542260; -.
DR Gramene; Zm00001eb330020_T001; Zm00001eb330020_P001; Zm00001eb330020.
DR Gramene; Zm00001eb330020_T004; Zm00001eb330020_P004; Zm00001eb330020.
DR Gramene; Zm00001eb330020_T006; Zm00001eb330020_P006; Zm00001eb330020.
DR KEGG; zma:542260; -.
DR MaizeGDB; 47586; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P11428; -.
DR OMA; DNYSDNP; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; P11428; baseline and differential.
DR Genevisible; P11428; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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:SF83; SUPEROXIDE DISMUTASE [CU-ZN] 2; 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; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..151
FT /note="Superoxide dismutase [Cu-Zn] 2"
FT /id="PRO_0000164141"
FT BINDING 44
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 55..144
FT /evidence="ECO:0000250"
SQ SEQUENCE 151 AA; 15104 MW; 6B1E8C703B17D216 CRC64;
MVKAVAVLAG TDVKGTIFFS QEGDGPTTVT GSISGLKPGL HGFHVHALGD TTNGCMSTGP
HFNPVGKEHG APEDEDRHAG DLGNVTAGED GVVNVNITDS QIPLAGPHSI IGRAVVVHAD
PDDLGKGGHE LSKSTGNAGG RVACGIIGLQ G
//
