ID   PPO_ZINOF               Reviewed;          10 AA.
AC   P85026;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 25.
DE   RecName: Full=Polyphenol oxidase;
DE            Short=PPO;
DE            EC=1.10.3.1;
DE   AltName: Full=Catechol oxidase;
DE   Flags: Fragment;
OS   Zingiber officinale (Ginger) (Amomum zingiber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=94328;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RC   TISSUE=Rhizome {ECO:0000269|Ref.1};
RA   Joseph A., Thayumanavan B., Manickam A., Panicker P.R.;
RT   "Purification and characterization of a polyphenol oxidase from the rhizome
RT   of Zingiber officinale.";
RL   Submitted (SEP-2006) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC       diquinones. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O;
CC         Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1;
CC         Evidence={ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5. Active from pH 3.0 to 8.0. The activity decreases
CC         sharply above pH 7.5. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. There is only a slight
CC         decrease in activity at 75 degrees Celsius and a sharp decrease in
CC         activity at 90 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed in the rhizome. Not detected in leaves.
CC       {ECO:0000269|Ref.1}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout rhizome development.
CC       {ECO:0000269|Ref.1}.
CC   -!- PTM: Glycosylated. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000269|Ref.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Oxidoreductase.
FT   CHAIN           1..>10
FT                   /note="Polyphenol oxidase"
FT                   /id="PRO_0000259621"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   10 AA;  946 MW;  38286BAAA87862C8 CRC64;
     EQGVGGDDGL