ID SODCP_POPTM Reviewed; 201 AA.
AC P36214;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Superoxide dismutase [Cu-Zn], chloroplastic;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODCP;
OS Populus tremuloides (Quaking aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7824654; DOI=10.1104/pp.106.3.1231;
RA Akkapeddi A.S., Shin D.I., Stanek M.T., Karnosky D.F., Podila G.K.;
RT "cDNA and derived amino acid sequence of the chloroplastic copper/zinc-
RT superoxide dismutase from aspen (Populus tremuloides).";
RL Plant Physiol. 106:1231-1232(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; U08097; AAA82127.1; -; mRNA.
DR AlphaFoldDB; P36214; -.
DR SMR; P36214; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 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; 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..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..201
FT /note="Superoxide dismutase [Cu-Zn], chloroplastic"
FT /id="PRO_0000032850"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 119..193
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 21552 MW; 7D154EBF1B2A9096 CRC64;
MASQTLVSPS PLSSPSLLRT SFSGVSVKLA PQFSTLATSN FKPLTVVAAA KKAVAVLKGQ
SRVEGSSTLH QDERQQQLMF VSLAYTQGFM VFTYMSMVIP QMGVSQQDHI LIQQVDTWCS
EDEIRHAGDL GNIVANAEGV AECRQSWQIR YHSLRPNSVV GRALVVHELQ DDLGKGGHEL
SLSTGNAGGR LACGVVGLTP V
//
