ID   PPOB_SOLLC              Reviewed;         596 AA.
AC   Q08304;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2008, entry version 53.
DE   RecName: Full=Polyphenol oxidase B, 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; Z12834; CAA78296.1; -; Genomic_DNA.
DR   PIR; S33540; S33540.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; Metal-binding; Oxidoreductase; Plastid;
KW   Thioether bond; Transit peptide.
FT   TRANSIT       1     87       Chloroplast (By similarity).
FT   CHAIN        88    596       Polyphenol oxidase B, chloroplastic.
FT                                /FTId=PRO_0000035911.
FT   METAL       181    181       Copper A (By similarity).
FT   METAL       199    199       Copper A (By similarity).
FT   METAL       208    208       Copper A (By similarity).
FT   METAL       329    329       Copper B (By similarity).
FT   METAL       333    333       Copper B (By similarity).
FT   METAL       371    371       Copper B (By similarity).
FT   DISULFID     98    114       By similarity.
FT   DISULFID    113    182       By similarity.
FT   CROSSLNK    185    199       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
SQ   SEQUENCE   596 AA;  67227 MW;  BD8553F7972FC7E8 CRC64;
     MASVVCNSSS STTTTTLKTP FTSLGSTPKP SQLFLHGKRN KTFKVSCKVI NNNGNQDETN
     SVDRRNVLLG LGGLYGVANA IPLAASATPI PSPDLKTCGR ATISDGPLVP YSCCPPPMPT
     NFDTIPYYKF PSMTKLRIRT PAHAVDEEYI AKYNLAISRM RDLDKTEPLN PLGFKQQANI
     HCAYCNGAYI IGGKELQVHN SWLFFPFHRW YLYFYERILG KLIDDPTFAL PYWNWDHPKG
     MRLPPMFDRE GSSLYDERRN QQVRNGTVLD LGSFGDKVET TQLQLMSNNL TLMYRQMVTN
     APCPLLFFGA PYVLGNNVEA PGTIETIPHI PVHIWAGTVR GSKFPNGDVS YGEDMGNFYS
     AGLDPVFYCH HGNVDRMWNE WKAIGGKRRD ISEKDWLNSE FFFYDEHKNP YRVKVRDCLD
     TKKMGYDYAP MPTPWRNFKP KSKASVGKVN TSTLPPANEV FPLAKMDKTI SFAINRPASS
     RTQQEKNEQE EMLTFNNIRY DNRGYIRFDV FLNVDNNVNA NELDKAEFAG SYTSLPHVHR
     AGENDHIAKV NFQLAITELL EDIGLEDEDT IAVTLVPKKG GEGISIENVE IKLVDC
//