ID   PPO_VITVI               Reviewed;         607 AA.
AC   P43311;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=Polyphenol oxidase, chloroplastic;
DE            Short=PPO;
DE            EC=1.10.3.1;
DE   AltName: Full=Catechol oxidase;
DE   Flags: Precursor;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sultana; TISSUE=Fruit;
RX   PubMed=7948897; DOI=10.1007/bf00039560;
RA   Dry I.B., Robinson S.P.;
RT   "Molecular cloning and characterisation of grape berry polyphenol
RT   oxidase.";
RL   Plant Mol. Biol. 26:495-502(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 104-442 IN COMPLEX WITH COPPER
RP   IONS, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS, AND COFACTOR.
RX   PubMed=20039636; DOI=10.1021/jf902939q;
RA   Virador V.M., Reyes Grajeda J.P., Blanco-Labra A., Mendiola-Olaya E.,
RA   Smith G.M., Moreno A., Whitaker J.R.;
RT   "Cloning, sequencing, purification, and crystal structure of Grenache
RT   (Vitis vinifera) polyphenol oxidase.";
RL   J. Agric. Food Chem. 58:1189-1201(2010).
CC   -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC       diquinones. {ECO:0000269|PubMed:20039636}.
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|PubMed:20039636};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:20039636};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:20039636};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; Z27411; CAA81798.1; -; mRNA.
DR   PDB; 2P3X; X-ray; 2.20 A; A=104-442.
DR   AlphaFoldDB; P43311; -.
DR   SMR; P43311; -.
DR   BRENDA; 1.10.3.1; 6671.
DR   EvolutionaryTrace; P43311; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0004097; F:catechol oxidase activity; EXP:UniProtKB.
DR   GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR   FunFam; 1.10.1280.10:FF:000007; Polyphenol oxidase, chloroplastic; 1.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR016213; Polyphenol_oxidase.
DR   InterPro; IPR022740; Polyphenol_oxidase_C.
DR   InterPro; IPR022739; Polyphenol_oxidase_cen.
DR   InterPro; IPR050316; Tyrosinase/Hemocyanin.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF12142; PPO1_DWL; 1.
DR   Pfam; PF12143; PPO1_KFDV; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PIRSF; PIRSF000290; PPO_plant; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
DR   PDBsum; 2P3X; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Plastid; Thioether bond; Thylakoid; Transit peptide.
FT   TRANSIT         1..103
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           104..607
FT                   /note="Polyphenol oxidase, chloroplastic"
FT                   /id="PRO_0000035920"
FT   REGION          39..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         190
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   BINDING         211
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   BINDING         220
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   BINDING         342
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   BINDING         346
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   BINDING         375
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   DISULFID        114..129
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   DISULFID        128..191
FT                   /evidence="ECO:0000269|PubMed:20039636"
FT   CROSSLNK        194..211
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           159..173
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           183..194
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           216..234
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           250..252
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           257..260
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           294..306
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           307..311
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           316..320
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           338..343
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           344..349
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          352..355
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   TURN            357..360
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           371..388
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           399..402
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          405..409
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          415..419
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   HELIX           420..423
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   TURN            426..430
FT                   /evidence="ECO:0007829|PDB:2P3X"
FT   STRAND          431..433
FT                   /evidence="ECO:0007829|PDB:2P3X"
SQ   SEQUENCE   607 AA;  67347 MW;  B9045598E69BC57B CRC64;
     MASLPWSLTT STAIANTTNI SAFPPSPLFQ RASHVPVARN RSRRFAPSKV SCNSANGDPN
     SDSTSDVRET SSGKLDRRNV LLGIGGLYGA AGGLGATKPL AFGAPIQAPD ISKCGTATVP
     DGVTPTNCCP PVTTKIIDFQ LPSSGSPMRT RPAAHLVSKE YLAKYKKAIE LQKALPDDDP
     RSFKQQANVH CTYCQGAYDQ VGYTDLELQV HASWLFLPFH RYYLYFNERI LAKLIDDPTF
     ALPYWAWDNP DGMYMPTIYA SSPSSLYDEK RNAKHLPPTV IDLDYDGTEP TIPDDELKTD
     NLAIMYKQIV SGATTPKLFL GYPYRAGDAI DPGAGTLEHA PHNIVHKWTG LADKPSEDMG
     NFYTAGRDPI FFGHHANVDR MWNIWKTIGG KNRKDFTDTD WLDATFVFYD ENKQLVKVKV
     SDCVDTSKLR YQYQDIPIPW LPKNTKAKAK TTTKSSKSGV AKAAELPKTT ISSIGDFPKA
     LNSVIRVEVP RPKKSRSKKE KEDEEEVLLI KGIELDRENF VKFDVYINDE DYSVSRPKNS
     EFAGSFVNVP HKHMKEMKTK TNLRFAINEL LEDLGAEDDE SVIVTIVPRA GGDDVTIGGI
     EIEFVSD
//