ID PPOE_SOLLC Reviewed; 587 AA. AC Q08307; Q41175; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 107. DE RecName: Full=Polyphenol oxidase E, 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Tiny tim; RX PubMed=1633491; DOI=10.1105/tpc.4.2.135; RA Shahar T., Hennig N., Gutfinger T., Hareven D., Lifschitz E.; RT "The tomato 66.3-kD polyphenoloxidase gene: molecular identification and RT developmental expression."; RL Plant Cell 4:135-147(1992). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z12837; CAA78299.1; -; Genomic_DNA. DR EMBL; S40548; AAB22610.1; -; Genomic_DNA. DR PIR; S33543; S33543. DR AlphaFoldDB; Q08307; -. DR SMR; Q08307; -. DR STRING; 4081.Q08307; -. DR PaxDb; 4081-Solyc08g074620-1-1; -. DR eggNOG; ENOG502QVBP; Eukaryota. DR InParanoid; Q08307; -. DR BioCyc; MetaCyc:MONOMER-16342; -. DR Proteomes; UP000004994; Unplaced. DR ExpressionAtlas; Q08307; 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..87 FT /note="Chloroplast" FT CHAIN 88..587 FT /note="Polyphenol oxidase E, chloroplastic" FT /id="PRO_0000035914" 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 328 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 332 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 363 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT DISULFID 98..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" FT CONFLICT 311..315 FT /note="PLGSE -> LWVLN (in Ref. 2; AAB22610)" FT /evidence="ECO:0000305" FT CONFLICT 410 FT /note="C -> V (in Ref. 2; AAB22610)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="L -> V (in Ref. 2; AAB22610)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="V -> I (in Ref. 2; AAB22610)" FT /evidence="ECO:0000305" FT CONFLICT 574 FT /note="E -> G (in Ref. 2; AAB22610)" FT /evidence="ECO:0000305" SQ SEQUENCE 587 AA; 66237 MW; A796AA1DD6454E3D CRC64; MSSSSSITTT LPLCTNKSLS SSFTTTNSSL LSKPSQLFLH GRRNQSFKVS CNANNVDKNP DAVDRRNVLL GLGGLYGAAN LAPLATAAPI PPPDLKSCGT AHVKEGVDVI YSCCPPVPDD IDSVPYYKFP SMTKLRIRPP AHAADEEYVA KYQLATSRMR ELDKDPFDPL GFKQQANIHC AYCNGAYKVG GKELQVHFSW LFFPFHRWYL YFYERILGSL INDPTFALPY WNWDHPKGMR IPPMFDREGS SLYDEKRNQN HRNGTIIDLG HFGKEVDTPQ LQIMTNNLTL MYRQMVTNAP CPSQFFGAAY PLGSEPSPGQ GTIENIPHTP VHIWTGDKPR QKNGEDMGNF YSAGLDPIFY CHHANVDRMW NEWKLIGGKR RDLTDKDWLN SEFFFYDENR NPYRVKVRDC LDSKKMGFDY APMPTPWRNF KPIRKSSSGK VNTASIAPVS KVFPLAKLDR AISFSITRPA SSRTTQEKNE QEEILTFNKI SYDDRNYVRF DVFLNVDKTV NADELDKAEF AGSYTSLPHV HGSNTNHVTS LTFKLAITEL LEDIGLEDED TIAVTLVPKA GGEEVSIESV EIKLEDC //