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   16-JUN-2009, entry version 56.
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; 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Tiny tim;
RX   MEDLINE=92338844; 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
RT   and 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: 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; Z12837; CAA78299.1; -; Genomic_DNA.
DR   EMBL; S40548; AAB22610.1; -; Genomic_DNA.
DR   PIR; S33543; S33543.
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.
FT   CHAIN        88    587       Polyphenol oxidase E, chloroplastic.
FT                                /FTId=PRO_0000035914.
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       328    328       Copper B (By similarity).
FT   METAL       332    332       Copper B (By similarity).
FT   METAL       363    363       Copper B (By similarity).
FT   DISULFID     98    114       By similarity.
FT   DISULFID    113    180       By similarity.
FT   CROSSLNK    183    197       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
FT   CONFLICT    311    315       PLGSE -> LWVLN (in Ref. 2; AAB22610).
FT   CONFLICT    410    410       C -> V (in Ref. 2; AAB22610).
FT   CONFLICT    541    541       L -> V (in Ref. 2; AAB22610).
FT   CONFLICT    567    567       V -> I (in Ref. 2; AAB22610).
FT   CONFLICT    574    574       E -> G (in Ref. 2; AAB22610).
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
//