ID   PPOF_SOLLC              Reviewed;         585 AA.
AC   Q08296;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Polyphenol oxidase F, 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; Z12838; CAA78300.1; -; Genomic_DNA.
DR   PIR; S33544; S33544.
DR   AlphaFoldDB; Q08296; -.
DR   SMR; Q08296; -.
DR   STRING; 4081.Q08296; -.
DR   PaxDb; 4081-Solyc08g074630-1-1; -.
DR   eggNOG; ENOG502QVBP; Eukaryota.
DR   InParanoid; Q08296; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q08296; 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:SF92; POLYPHENOL OXIDASE F, 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..86
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           87..585
FT                   /note="Polyphenol oxidase F, chloroplastic"
FT                   /id="PRO_0000035915"
FT   BINDING         179
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         197
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         326
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         330
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         361
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        113..180
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        183..197
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   585 AA;  66183 MW;  6C8C7C1D2F00DD5D CRC64;
     MSSSTPNTLP LLSTNKSLSS PFTNNHSTFL SKPSQPFLHG RRCQSFKVSC NVGEHDKNLD
     AVDRRNVLLG LGGFYGAANL APLASAAPIP PPDLKSCGVA HIDDKGTEVS YSCCPPVPDD
     IDSVPYYKFP PMTKLRIRPP AHAADEEYVA KYQLATSRMR ELDKDPFDPL GFKQQANIHC
     AYCNGAYKIG GKELQVHFSW LFFPFHRWYL YFYERILGSL INDPTFALPY WNWDHPKGMR
     IPPMFDREGS SLYDEKRNQN HRNGTIIDLG HFGKDVRTPQ LQIMTNNLTL MYRQMVTNAP
     CPSQFFGAPL GSDPEPGMGT IENIPHTPVH IWTGDSPRQG HGEDMGNFYS AGLDPLFYCH
     HANVDRMWNE WKLIGGKRRD LSNKDWLNSE FFFYDENRNP YRVKVRDCLD SKKMGFDYPP
     MPTPWRNFKP IRRSSSGKVN TASIAPVSKV FPLAKLDRAI SFSLTRPASS RTTQEKNEQQ
     EILTFNKMAY DDTKYVRFDV FLNVDKTVNA EELDKAEFAG SYTSLPHVHG NNDNHVKDVT
     FTLAITELLE DIGLEDEDTI AVTLVPKVGG EGVSIESVEI KLEDC
//