ID   PPOD_SOLLC              Reviewed;         591 AA.
AC   Q08306;
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 D, 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; Z12836; CAA78298.1; -; Genomic_DNA.
DR   PIR; S33542; S33542.
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    591       Polyphenol oxidase D, chloroplastic.
FT                                /FTId=PRO_0000035913.
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   591 AA;  66529 MW;  083C08429E80C85F CRC64;
     MASLCSNSST TSLKTPFTSL GSTPKPCQLF LHGKRNKAFK VSCKVTNTNG NQDETNSVDR
     RNVLLGLGGL YGVANAIPLA ASAAPTPPPD LSSCSIARID ENQVVSYSCC APKPDDMEKV
     PYYKFPSMTK LRVRQPAHEA DEEYIAKYNV SVTKMRDLDK TQPLNPIGFK QQANIHCAYC
     NGAYRIGGKE LQVHNSWLFF PFHRWYLYFY ESNAGKLIDD PTFALPYWNW DHPKGMRFPA
     MYDREGTFLF DETRDQSHRN GTVIDLGFFG NEVETTQLQM MSNNLTLMYR QMVTNAPCPR
     MFFGDLMISG ITLNSPGTIE NIPHGPVHIW SGTVRGSTLP NGAISKRGEY GHFYSAGLDP
     VFFCHHSNVD RMWSEWKATG GKRTDITHKD WLNSEFFFYD ENENPYRVKV RDCLDTKKMG
     YDYKPMRTPW RNFKPLTKAS AGKVNTSSIP PVSQAFPLAK LDKAVSFSIN RPTSSRTPQE
     KNAQEEMLTF NSIRYDNRGY IRFDVFLNVD NNVNANELDK AEFAGSYTSL PHVHRAGETN
     HIATVDFQLA ITELLEDIGL EDEDTIAVTL VPKRGGEGIS IENATISLAD C
//