ID   PPO_SPIOL               Reviewed;         639 AA.
AC   P43310;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Polyphenol oxidase, chloroplastic;
DE            Short=PPO;
DE            EC=1.10.3.1;
DE   AltName: Full=Catechol oxidase;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hybrid 424; TISSUE=Leaf;
RX   PubMed=7794929; DOI=10.1021/bi00025a022;
RA   Hind G., Marshak D.R., Coughlan S.J.;
RT   "Spinach thylakoid polyphenol oxidase: cloning, characterization, and
RT   relation to a putative protein kinase.";
RL   Biochemistry 34:8157-8164(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC       diquinones.
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   -!- 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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; U19270; AAC49041.1; -; mRNA.
DR   EMBL; Z66559; CAA91448.1; -; mRNA.
DR   AlphaFoldDB; P43310; -.
DR   SMR; P43310; -.
DR   PRIDE; P43310; -.
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; 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   2: Evidence at transcript level;
KW   Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW   Plastid; Thioether bond; Thylakoid; Transit peptide.
FT   TRANSIT         1..101
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           102..639
FT                   /note="Polyphenol oxidase, chloroplastic"
FT                   /id="PRO_0000035918"
FT   REGION          35..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         193
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         214
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         223
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         354
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         358
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         388
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        111..127
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        126..194
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        197..214
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   639 AA;  73237 MW;  56917BBF12F5162A CRC64;
     MATLSSPTII TTTSILLNNP FLPKTPQLSA HHHRGVRSVN GKVSCQTKNN NGNDENNQFQ
     LIQNPNTNTP YLLDRRNILL GLGGMYAALG SEGANYYNTL AAPILPDVEK CTLSDALWDG
     SVGDHCCPPP FDLNITKDFE FKNYHNHVKK VRRPAHKAYE DQEWLNDYKR AIAIMKSLPM
     SDPRSHMQQA RVHCAYCDGS YPVLGHNDTR LEVHASWLFP SFHRWYLYFY ERILGKLINK
     PDFALPYWNW DHRDGMRIPE IFKEMDSPLF DPNRNTNHLD KMMNLSFVSD EEGSDVNEDD
     QYEENILLMR KAMVYPSVSD DPNKAELFLG SPYRAGDKME GDVSGAGILE RMPHNSVHVW
     TRSNTIKGNQ DMGAFWSAGR DPLFYCHHSN VDRMWSLWTD VLHGGNFPKT PEYDDYRNAY
     FYFYDENANP VRVYVRDSFD TERLGYKYED QELPWMSITQ QQQQQQRQQQ RQPLLGGRLK
     TRTFSLVKKV LTELKVMLPL PLKYSVIKTK VDRPKKSRTK EDKLEHEEVL VINFKLGKSK
     DFIKFDVYIN DGTDYKPEDK TKINLEYAGS FTSLTHGGGG GGGDMSHMAE EDMGKNTVLK
     LALNQLLEDL DATDDDSIQV TIVPKSGTDS IVITGIDIE