ID   PPOC_SOLLC              Reviewed;         626 AA.
AC   Q08305;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Polyphenol oxidase C, 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; Z12835; CAA78297.1; -; Genomic_DNA.
DR   PIR; S33541; S33541.
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     83       Chloroplast (By similarity).
FT   CHAIN        84    626       Polyphenol oxidase C, chloroplastic.
FT                                /FTId=PRO_0000035912.
FT   METAL       176    176       Copper A (By similarity).
FT   METAL       194    194       Copper A (By similarity).
FT   METAL       203    203       Copper A (By similarity).
FT   METAL       324    324       Copper B (By similarity).
FT   METAL       328    328       Copper B (By similarity).
FT   METAL       366    366       Copper B (By similarity).
FT   DISULFID     94    110       By similarity.
FT   DISULFID    109    177       By similarity.
FT   CROSSLNK    180    194       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
SQ   SEQUENCE   626 AA;  70333 MW;  712D8F9E82E7A3DB CRC64;
     MASLCSNSST TSLKTPFTSL GSTPKPCQLF LHGKRNKAFK VSCKVTNTNG NQDETNSVDR
     RNVLLGLGGL YGVANAIPLA ASAAPTPPPD LSSCSIARID ENQVVSYSCC APKPDDMEKV
     PYYKFPSMTK LRVRQPAHEA DEEYIAKYNC AVTKMKDLDK TQPDNPIGFK QQANIHCAYC
     NGGYSIDGKV LQVHNSWLFF PFHRWYLYFY ERILGSLIDD PTFGLPFWNW DHPKGMRFPP
     MFDVPGTALY DERRGDQIHN GNGIDLGYFG DQVETTQLQL MTNNLTLMYR QLVTNSPCPL
     MSLVDLTLFG STVEDAGTVE NIPHSPVHIW VGTRRGSVLP VGKISNGEDM GNFYSAGLDP
     LFYCHHSNVD RMWNEWKATG GKRTDIQNKD WLNSEFFFYD ENGNPFKVRV RDCLDTKKMG
     YDYHATATPW RNFKPKTKAS AGKVNTGSIP PESQVFPLAK LDKAISFSIN RPASSRTQQE
     KNAQEEVLTF NAIKYDNRDY IRFDVFLNVD NNVNANELDK AEFAGSYTSL PHVHRVGDPK
     HTATATLRLA ITELLEDIGL EDEDTIAVTL VPKKGDISIG GVEIKLAIVK LVCVVNLLTL
     QLNKDRFCYD SVFVCWFVCL FFNFHV
//