PPO_VITVI
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 03-AUG-2022, entry version 107.
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 PDBsum; 2P3X; -.
DR AlphaFoldDB; P43311; -.
DR SMR; P43311; -.
DR PRIDE; P43311; -.
DR BRENDA; 1.10.3.1; 6671.
DR EvolutionaryTrace; P43311; -.
DR ExpressionAtlas; P43311; baseline and differential.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1280.10; -; 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; IPR002227; Tyrosinase_Cu-bd.
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; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
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 46..68
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 STRAND 136..138
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..309
FT /evidence="ECO:0007829|PDB:2P3X"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2P3X"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:2P3X"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:2P3X"
FT HELIX 342..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..385
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
