ID   PPO_VICFA               Reviewed;         606 AA.
AC   Q06215;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Polyphenol oxidase A1, chloroplastic;
DE            Short=PPO;
DE            EC=1.10.3.1;
DE   AltName: Full=Catechol oxidase;
DE   Flags: Precursor;
OS   Vicia faba (Broad bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   MEDLINE=93004477; PubMed=1391768; DOI=10.1007/BF00014492;
RA   Cary J.W., Lax A.R., Flurkey W.H.;
RT   "Cloning and characterization of cDNAs coding for Vicia faba
RT   polyphenol oxidase.";
RL   Plant Mol. Biol. 20:245-253(1992).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 93-119.
RC   TISSUE=Leaf;
RX   PubMed=16667057;
RA   Flurkey W.H.;
RT   "Polypeptide composition and amino-terminal sequence of broad bean
RT   polyphenol oxidase.";
RL   Plant Physiol. 91:481-483(1989).
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; Z11702; CAA77764.1; -; mRNA.
DR   PIR; S24758; S24758.
DR   BRENDA; 1.10.3.1; 30.
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   1: Evidence at protein level;
KW   Chloroplast; Copper; Direct protein sequencing; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Plastid; Thioether bond;
KW   Transit peptide.
FT   TRANSIT       1     92       Chloroplast.
FT   CHAIN        93    606       Polyphenol oxidase A1, chloroplastic.
FT                                /FTId=PRO_0000035919.
FT   METAL       181    181       Copper A (By similarity).
FT   METAL       202    202       Copper A (By similarity).
FT   METAL       211    211       Copper A (By similarity).
FT   METAL       333    333       Copper B (By similarity).
FT   METAL       337    337       Copper B (By similarity).
FT   METAL       367    367       Copper B (By similarity).
FT   DISULFID    103    121       By similarity.
FT   DISULFID    120    182       By similarity.
FT   CROSSLNK    185    202       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
SQ   SEQUENCE   606 AA;  68541 MW;  FC539F9F041B503C CRC64;
     MTSISALSFI STINVSSNSK ISHSSVYPFL QKQHQSSKLR KPKRQVTCSS NNNQNNPKEE
     QELSNIVGHR RNVLIGLGGI YGTLATNPSA LASPISPPDL SKCVPPSDLP SGTTPPNINC
     CPPYSTKITD FKFPSNQPLR VRQAAHLVDN EFLEKYKKAT ELMKALPSND PRNFTQQANI
     HCAYCDGAYS QIGFPDLKLQ VHGSWLFFPF HRWYLYFYER ILGSLINDPT FALPFWNYDA
     PDGMQLPTIY ADKASPLYDE LRNASHQPPT LIDLNFCDIG SDIDRNELIK TNLSIMYRQV
     YSNGKTSRLF LGNPYRAGDA EPQGAGSIEN VPHAPVHTWT GDNTQTNIED MGIFYSAARD
     PIFYSHHSNV DRLWYIWKTL GGKKHDFTDK DWLESGFLFY DENKNLVRVN VKDSLDIDKL
     GYAYQDVPIP WEKAKPVPRR TKVQKLVEVE VNDGNLRKSP TIFLVRQQSP RKYVTFPLVL
     NNKVSAIVKR PKKLRSKKEK EEEEEVLVIE GIEFYMNIAI KFDVYINDED DKVGAGNTEF
     AGSFVNIPHS AHGHKNKKII TSLRLGITDL LEDLHVEGDD NIVVTLVPKC GSGQVKINNV
     EIVFED
//