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 16-JUN-2009, entry version 55. 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; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. VFNT Cherry; RX MEDLINE=93257620; 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: 2 catechol + O(2) = 2 1,2-benzoquinone + 2 CC H(2)O. CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. CC -!- SIMILARITY: Belongs to the tyrosinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z12838; CAA78300.1; -; Genomic_DNA. DR PIR; S33544; S33544. DR BRENDA; 1.10.3.1; 281054. DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell. DR GO; GO:0004097; F:catechol oxidase activity; IEA:EC. DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR016213; Polyphenol_Oxase_pln. DR InterPro; IPR002227; Tyrosinase. DR Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1. DR Pfam; PF00264; Tyrosinase; 1. DR PIRSF; PIRSF000290; PPO_plant; 1. DR PRINTS; PR00092; TYROSINASE. 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; Thioether bond; Transit peptide. FT TRANSIT 1 86 Chloroplast (By similarity). FT CHAIN 87 585 Polyphenol oxidase F, chloroplastic. FT /FTId=PRO_0000035915. FT METAL 179 179 Copper A (By similarity). FT METAL 197 197 Copper A (By similarity). FT METAL 206 206 Copper A (By similarity). FT METAL 326 326 Copper B (By similarity). FT METAL 330 330 Copper B (By similarity). FT METAL 361 361 Copper B (By similarity). FT DISULFID 97 114 By similarity. FT DISULFID 113 180 By similarity. FT CROSSLNK 183 197 2'-(S-cysteinyl)-histidine (Cys-His) (By FT similarity). 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 //