SODCP_SOLLC
ID SODCP_SOLLC Reviewed; 217 AA.
AC P14831;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Superoxide dismutase [Cu-Zn], chloroplastic;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODCP.2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Sherry; TISSUE=Leaf;
RX AGRICOLA=IND92000006; DOI=10.1007/BF00017461;
RA Perl-Treves R., Nacmias B., Aviv D., Zeelon E.P., Galun E.;
RT "Isolation of two cDNA clones from tomato containing two different
RT superoxide dismutase sequences.";
RL Plant Mol. Biol. 11:609-623(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8075404; DOI=10.1007/bf00028883;
RA Kardish N., Magal N., Aviv D., Galun E.;
RT "The tomato gene for the chloroplastic Cu,Zn superoxide dismutase:
RT regulation of expression imposed in transgenic tobacco plants by a short
RT promoter.";
RL Plant Mol. Biol. 25:887-897(1994).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M37151; AAA34195.1; -; mRNA.
DR EMBL; X14041; CAA32200.1; -; mRNA.
DR EMBL; X77175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X77176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S48021; S48021.
DR PDB; 3HOG; X-ray; 1.85 A; A=64-217.
DR PDB; 3KM1; X-ray; 2.00 A; A/B=64-217.
DR PDB; 3KM2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=64-217.
DR PDB; 3MKG; X-ray; 2.20 A; A/B=64-217.
DR PDB; 3PU7; X-ray; 1.80 A; A/B=64-217.
DR PDB; 3S0P; X-ray; 3.00 A; A/B/C/D/E/F/G/H=64-217.
DR PDBsum; 3HOG; -.
DR PDBsum; 3KM1; -.
DR PDBsum; 3KM2; -.
DR PDBsum; 3MKG; -.
DR PDBsum; 3PU7; -.
DR PDBsum; 3S0P; -.
DR AlphaFoldDB; P14831; -.
DR SMR; P14831; -.
DR STRING; 4081.Solyc11g066390.1.1; -.
DR Allergome; 11322; Sola l SOD.
DR PaxDb; P14831; -.
DR eggNOG; KOG0441; Eukaryota.
DR InParanoid; P14831; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P14831; baseline and differential.
DR GO; GO:0009507; C:chloroplast; 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; -; 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; Disulfide bond;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT CHAIN 64..217
FT /note="Superoxide dismutase [Cu-Zn], chloroplastic"
FT /id="PRO_0000032845"
FT BINDING 109
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 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 120..209
FT /evidence="ECO:0000250"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:3PU7"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3MKG"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:3HOG"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3PU7"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3KM2"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:3PU7"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3PU7"
SQ SEQUENCE 217 AA; 22228 MW; 3FC14252760CF2B0 CRC64;
MAAHSIFTTT STTNSFLYPI SSSSSSPNIN SSFLGVSLNV NAKFGQSLTL YAVTTPKPLT
VFAATKKAVA VLKGNSNVEG VVTLSQDDDG PTTVNVRITG LAPGLHGFHL HEYGDTTNGC
MSTGAHFNPN KLTHGAPGDE IRHAGDLGNI VANADGVAEV TLVDNQIPLT GPNSVVGRAL
VVHELEDDLG KGGHELSLTT GNAGGRLACG VVGLTPI
