PPOF_SOLLC
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 03-AUG-2022, entry version 98.
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.Solyc08g074630.1.1; -.
DR PaxDb; Q08296; -.
DR PRIDE; Q08296; -.
DR eggNOG; ENOG502QVBP; Eukaryota.
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; -; 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..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
