ID   PPOD_SOLLC              Reviewed;         591 AA.
AC   Q08306;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Polyphenol oxidase D, 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; Z12836; CAA78298.1; -; Genomic_DNA.
DR   PIR; S33542; S33542.
DR   AlphaFoldDB; Q08306; -.
DR   SMR; Q08306; -.
DR   STRING; 4081.Q08306; -.
DR   InParanoid; Q08306; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q08306; 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; Di-copper center containing domain from catechol oxidase; 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   PANTHER; PTHR11474:SF112; POLYPHENOL OXIDASE D, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
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; Di-copper centre-containing domain; 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..591
FT                   /note="Polyphenol oxidase D, chloroplastic"
FT                   /id="PRO_0000035913"
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   591 AA;  66529 MW;  083C08429E80C85F CRC64;
     MASLCSNSST TSLKTPFTSL GSTPKPCQLF LHGKRNKAFK VSCKVTNTNG NQDETNSVDR
     RNVLLGLGGL YGVANAIPLA ASAAPTPPPD LSSCSIARID ENQVVSYSCC APKPDDMEKV
     PYYKFPSMTK LRVRQPAHEA DEEYIAKYNV SVTKMRDLDK TQPLNPIGFK QQANIHCAYC
     NGAYRIGGKE LQVHNSWLFF PFHRWYLYFY ESNAGKLIDD PTFALPYWNW DHPKGMRFPA
     MYDREGTFLF DETRDQSHRN GTVIDLGFFG NEVETTQLQM MSNNLTLMYR QMVTNAPCPR
     MFFGDLMISG ITLNSPGTIE NIPHGPVHIW SGTVRGSTLP NGAISKRGEY GHFYSAGLDP
     VFFCHHSNVD RMWSEWKATG GKRTDITHKD WLNSEFFFYD ENENPYRVKV RDCLDTKKMG
     YDYKPMRTPW RNFKPLTKAS AGKVNTSSIP PVSQAFPLAK LDKAVSFSIN RPTSSRTPQE
     KNAQEEMLTF NSIRYDNRGY IRFDVFLNVD NNVNANELDK AEFAGSYTSL PHVHRAGETN
     HIATVDFQLA ITELLEDIGL EDEDTIAVTL VPKRGGEGIS IENATISLAD C
//