ID   SODCP_PEA               Reviewed;         202 AA.
AC   P11964;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Superoxide dismutase [Cu-Zn], chloroplastic;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODCP; Synonyms=SOD2;
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=2845417; DOI=10.1073/pnas.85.20.7661;
RA   Scioli J.R., Zilinskas B.A.;
RT   "Cloning and characterization of a cDNA encoding the chloroplastic
RT   copper/zinc-superoxide dismutase from pea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7661-7665(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2102887; DOI=10.1007/bf00016130;
RA   Isin S.H., Burke J.J., Allen R.D.;
RT   "Sequence divergence of pea Cu/Zn superoxide dismutase II cDNAs.";
RL   Plant Mol. Biol. 15:789-791(1990).
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: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; J04087; AAA33688.1; -; mRNA.
DR   EMBL; X56435; CAA39819.1; -; mRNA.
DR   PIR; A30204; DSPMCZ.
DR   AlphaFoldDB; P11964; -.
DR   SMR; P11964; -.
DR   BRENDA; 1.15.1.1; 4872.
DR   GO; GO:0009507; C:chloroplast; 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; Chloroplast; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Plastid; Transit peptide; Zinc.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT   CHAIN           49..202
FT                   /note="Superoxide dismutase [Cu-Zn], chloroplastic"
FT                   /id="PRO_0000032848"
FT   BINDING         94
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..194
FT                   /evidence="ECO:0000250"
FT   VARIANT         55
FT                   /note="S -> A"
SQ   SEQUENCE   202 AA;  20626 MW;  677BF4F185533A31 CRC64;
     MASQTLVSPS PLSSHSLLRT SFSGVSVKLA PQFSTLATSN FKPLTVVAAA KKAVSVLKGT
     SAVEGVVTLT QDDEGPTTVN VRITGLTPGL HGFHLHEYGD TTNGCISTGP HFNPNKLTHG
     APEDEIRHAG DLGNIVANAE GVAEATIVDN QIPLTGPNSV VGRALVVHEL QDDLGKGGHE
     LSLSTGNAGG RLACGVVGLT PV