PPOC_SOLLC
ID PPOC_SOLLC Reviewed; 626 AA.
AC Q08305;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Polyphenol oxidase C, chloroplastic;
DE Short=PPO;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase;
DE Flags: Precursor;
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 [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry;
RX PubMed=8098228; DOI=10.1007/bf00023601;
RA Newman S.M., Eannetta N.T., Yu H., Prince J.P., de Vicente M.C.,
RA Tanksley S.D., Steffens J.C.;
RT "Organisation of the tomato polyphenol oxidase gene family.";
RL Plant Mol. Biol. 21:1035-1051(1993).
CC -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC diquinones.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O;
CC Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; Z12835; CAA78297.1; -; Genomic_DNA.
DR PIR; S33541; S33541.
DR AlphaFoldDB; Q08305; -.
DR SMR; Q08305; -.
DR PRIDE; Q08305; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q08305; baseline and differential.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000290; PPO_plant; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW Plastid; Reference proteome; Thioether bond; Thylakoid; Transit peptide.
FT TRANSIT 1..83
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 84..626
FT /note="Polyphenol oxidase C, chloroplastic"
FT /id="PRO_0000035912"
FT BINDING 176
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 324
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 328
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 94..110
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 109..177
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 180..194
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 626 AA; 70333 MW; 712D8F9E82E7A3DB CRC64;
MASLCSNSST TSLKTPFTSL GSTPKPCQLF LHGKRNKAFK VSCKVTNTNG NQDETNSVDR
RNVLLGLGGL YGVANAIPLA ASAAPTPPPD LSSCSIARID ENQVVSYSCC APKPDDMEKV
PYYKFPSMTK LRVRQPAHEA DEEYIAKYNC AVTKMKDLDK TQPDNPIGFK QQANIHCAYC
NGGYSIDGKV LQVHNSWLFF PFHRWYLYFY ERILGSLIDD PTFGLPFWNW DHPKGMRFPP
MFDVPGTALY DERRGDQIHN GNGIDLGYFG DQVETTQLQL MTNNLTLMYR QLVTNSPCPL
MSLVDLTLFG STVEDAGTVE NIPHSPVHIW VGTRRGSVLP VGKISNGEDM GNFYSAGLDP
LFYCHHSNVD RMWNEWKATG GKRTDIQNKD WLNSEFFFYD ENGNPFKVRV RDCLDTKKMG
YDYHATATPW RNFKPKTKAS AGKVNTGSIP PESQVFPLAK LDKAISFSIN RPASSRTQQE
KNAQEEVLTF NAIKYDNRDY IRFDVFLNVD NNVNANELDK AEFAGSYTSL PHVHRVGDPK
HTATATLRLA ITELLEDIGL EDEDTIAVTL VPKKGDISIG GVEIKLAIVK LVCVVNLLTL
QLNKDRFCYD SVFVCWFVCL FFNFHV
