ID   PPOA_SOLLC              Reviewed;         630 AA.
AC   Q08303;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Polyphenol oxidase A, 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.
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DR   EMBL; Z12833; CAA78295.1; -; Genomic_DNA.
DR   PIR; S33539; S33539.
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     87       Chloroplast (By similarity).
FT   CHAIN        88    630       Polyphenol oxidase A, chloroplastic.
FT                                /FTId=PRO_0000035910.
FT   METAL       180    180       Copper A (By similarity).
FT   METAL       198    198       Copper A (By similarity).
FT   METAL       207    207       Copper A (By similarity).
FT   METAL       328    328       Copper B (By similarity).
FT   METAL       332    332       Copper B (By similarity).
FT   METAL       370    370       Copper B (By similarity).
FT   DISULFID     98    114       By similarity.
FT   DISULFID    113    181       By similarity.
FT   CROSSLNK    184    198       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
SQ   SEQUENCE   630 AA;  70616 MW;  821F3297879326F1 CRC64;
     MASLCSNSSS TSLKTPFTSS TTCLSSTPTA SQLFLHGKRN KTFKVSCKVT NTNGNQDETN
     SVDRRNVLLG LGGLYGVANA IPLAASAAPT PPPDLSSCNK PKINATTEVP YFCCAPKPDD
     MSKVPYYKFP SVTKLRIRPP AHALDEAYIA KYNLAISRMK DLDKTQPDNP IGFKQQANIH
     CAYCNGGYSI DGKVLQVHNS WLFFPFHRWY LYFYERILGS LIDDPTFGLP FWNWDHPKGM
     RFPPMFDVPG TALYDERRGD QIHNGNGIDL GYFGDQVETT QLQLMTNNLT LMYRQLVTNS
     PCPLMSLVDL TLFGSTVEDA GTVENIPHSP VHIWVGTRRG SVLPVGKISN GEDMGNFYSA
     GLDPLFYCHH SNVDRMWNEW KATGGKRTDI QNKDWLNSEF FFYDENGNPF KVRVRDCLDT
     KKMGYDYHAT ATPWRNFKPK TKASAGKVNT GSIPPESQVF PLAKLDKAIS FSINRPASSR
     TQQEKNAQEE VLTFNAIKYD NRDYIRFDVF LNVDNNVNAN ELDKAEFAGS YTSLPHVHRV
     GDPKHTATAT LRLAITELLE DIGLEDEDTI AVTLVPKKGD ISIGGVEIKL AIVKLVCVVN
     LLTLQLNKDR FCYDSVFVCW FVCLFFNFHV
//