ID   PPOB_SOLTU              Reviewed;         588 AA.
AC   Q06355;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Catechol oxidase B, chloroplastic;
DE            EC=1.10.3.1;
DE   AltName: Full=Polyphenol oxidase;
DE            Short=PPO;
DE   Flags: Precursor; Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Katahdin; TISSUE=Leaf;
RX   MEDLINE=93144692; PubMed=7678763; DOI=10.1007/BF00039618;
RA   Hunt M.D., Eannetta N.T., Yu H., Newman S.M., Steffens J.C.;
RT   "cDNA cloning and expression of potato polyphenol oxidase.";
RL   Plant Mol. Biol. 21:59-68(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; M95197; AAA02879.1; -; mRNA.
DR   PIR; S30929; S30929.
DR   BRENDA; 1.10.3.1; 296.
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   2: Evidence at transcript level;
KW   Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW   Plastid; Thioether bond; Transit peptide.
FT   TRANSIT      <1     88       Chloroplast (Potential).
FT   CHAIN        89    588       Catechol oxidase B, chloroplastic.
FT                                /FTId=PRO_0000035917.
FT   METAL       180    180       Copper A (By similarity).
FT   METAL       198    198       Copper A (By similarity).
FT   METAL       207    207       Copper A (By similarity).
FT   METAL       329    329       Copper B (By similarity).
FT   METAL       333    333       Copper B (By similarity).
FT   METAL       364    364       Copper B (By similarity).
FT   DISULFID     99    115       By similarity.
FT   DISULFID    114    181       By similarity.
FT   CROSSLNK    184    198       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   588 AA;  66241 MW;  A7E25383273428CC CRC64;
     SSSSTTTIPL CTNKSLSSSF TTNNSSFLSK PSQLFLHGRR NQSFKVSCNA NNNVGEHDKN
     LDTVDRRNVL LGLGGLYGAA NLAPLASASP IPPPDLKSCG VAHVTEGVDV TYSCCPPVPD
     DIDSVPYYKF PPMTKLRIRP PAHAADEEYV AKYQLATSRM RELDKDSFDP LGFKQQANIH
     CAYCNGAYKV GGKELQVHFS WLFFPFHRWY LYFYERILGS LINDPTFALP YWNWDHPKGM
     RIPPMFDREG SSLYDDKRNQ NHRNGTIIDL GHFGQEVDTP QLQIMTNNLT LMYRQMVTNA
     PCPSQFFGAA YPLGTEPSPG MGTIENIPHT PVHIWTGDSP RQKNGENMGN FYSAGLDPIF
     YCHHANVDRM WDEWKLIGGK RRDLSNKDWL NSEFFFYDEN RNPYRVKVRD CLDSKKMGFS
     YAPMPTPWRN FKPIRKTTAG KVNTASIAPV TKVFPLAKLD RAISFSITRP ASSRTTQEKN
     EQEEILTFNK VAYDDTKYVR FDVFLNVDKT VNADELDKAE FAGSYTSLPH VHGNNTNHVT
     SVTFKLAITE LLEDNGLEDE DTIAVTLVPK VGGEGVSIES VEIKLEDC
//