SODCP_SPIOL
ID SODCP_SPIOL Reviewed; 222 AA.
AC P07505;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Superoxide dismutase [Cu-Zn], chloroplastic;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODCP;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Sakamoto A., Ohsuga H., Wakaura M., Mitsukawa N., Hibino T., Masumura T.,
RA Sasaki Y., Tanaka K.;
RT "cDNA cloning and expression of the plastidic copper/zinc-superoxide
RT dismutase from spinach (Spinacia oleracea L.) leaves.";
RL Plant Cell Physiol. 34:965-968(1993).
RN [2]
RP PROTEIN SEQUENCE OF 69-222.
RX PubMed=3519601; DOI=10.1093/oxfordjournals.jbchem.a135596;
RA Kitagawa Y., Tsunasawa S., Tanaka N., Katsube Y., Sakiyama F., Asada K.;
RT "Amino acid sequence of copper,zinc-superoxide dismutase from spinach
RT leaves.";
RL J. Biochem. 99:1289-1298(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS.
RX PubMed=1880134; DOI=10.1093/oxfordjournals.jbchem.a123407;
RA Kitagawa Y., Tanaka N., Hata Y., Kusunoki M., Lee G.-P., Katsube Y.,
RA Asada K., Aibara S., Morita Y.;
RT "Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at
RT 2.0-A resolution.";
RL J. Biochem. 109:477-485(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;
CC Evidence={ECO:0000269|PubMed:1880134};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:1880134};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1880134};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1880134};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1880134}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; D10244; BAA01088.1; -; mRNA.
DR PIR; JQ0940; DSSPCZ.
DR PDB; 1SRD; X-ray; 2.00 A; A/B/C/D=69-222.
DR PDBsum; 1SRD; -.
DR AlphaFoldDB; P07505; -.
DR SMR; P07505; -.
DR EvolutionaryTrace; P07505; -.
DR GO; GO:0009507; C:chloroplast; IDA:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Chloroplast; Copper; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Plastid; Transit peptide;
KW Zinc.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:3519601"
FT CHAIN 69..222
FT /note="Superoxide dismutase [Cu-Zn], chloroplastic"
FT /id="PRO_0000032852"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 116
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 131
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:1880134"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1880134"
FT DISULFID 125..214
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1SRD"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1SRD"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1SRD"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1SRD"
SQ SEQUENCE 222 AA; 22567 MW; 900E4061653575C1 CRC64;
MAAHTILASA PSHTTFSLIS PFSSTPTNAL SSSLQSSSFN GLSFKLSPTT QSLSLSTSAA
SKPLTIVAAT KKAVAVLKGT SNVEGVVTLT QEDDGPTTVN VRISGLAPGK HGFHLHEFGD
TTNGCMSTGP HFNPDKKTHG APEDEVRHAG DLGNIVANTD GVAEATIVDN QIPLTGPNSV
VGRALVVHEL EDDLGKGGHE LSPTTGNAGG RLACGVVGLT PV
