SODC_PEA
ID SODC_PEA Reviewed; 152 AA.
AC Q02610;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SODCC;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16668351; DOI=10.1104/pp.96.4.1391;
RA White D.A., Zilinskas B.A.;
RT "Nucleotide sequence of a complementary DNA encoding pea cytosolic
RT copper/zinc superoxide dismutase.";
RL Plant Physiol. 96:1391-1392(1991).
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; M63003; AAA33659.1; -; mRNA.
DR PIR; T06570; T06570.
DR AlphaFoldDB; Q02610; -.
DR SMR; Q02610; -.
DR EnsemblPlants; Psat3g008560.1; Psat3g008560.1.cds; Psat3g008560.
DR EnsemblPlants; Psat3g008560.2; Psat3g008560.2.cds; Psat3g008560.
DR EnsemblPlants; Psat3g008560.3; Psat3g008560.3.cds; Psat3g008560.
DR EnsemblPlants; Psat3g008560.4; Psat3g008560.4.cds; Psat3g008560.
DR EnsemblPlants; Psat3g008560.6; Psat3g008560.6.cds; Psat3g008560.
DR Gramene; Psat3g008560.1; Psat3g008560.1.cds; Psat3g008560.
DR Gramene; Psat3g008560.2; Psat3g008560.2.cds; Psat3g008560.
DR Gramene; Psat3g008560.3; Psat3g008560.3.cds; Psat3g008560.
DR Gramene; Psat3g008560.4; Psat3g008560.4.cds; Psat3g008560.
DR Gramene; Psat3g008560.6; Psat3g008560.6.cds; Psat3g008560.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..152
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164152"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 15323 MW; C61281A0D282C3B3 CRC64;
MVKAVAVLSN SNEVSGTINF SQEGNGPTTV TGTLAGLKPG LHGFHIHALG DTTNGCISTG
PHFNPNGKEH GAPEDETRHA GDLGNINVGD DGTVSFTITD NHIPLTGTNS IIGRAVVVHA
DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
