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   24-JAN-2024, entry version 102.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Katahdin; TISSUE=Leaf;
RX   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:
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; M95197; AAA02879.1; -; mRNA.
DR   PIR; S30929; S30929.
DR   AlphaFoldDB; Q06355; -.
DR   SMR; Q06355; -.
DR   STRING; 4113.Q06355; -.
DR   PaxDb; 4113-PGSC0003DMT400076054; -.
DR   eggNOG; ENOG502QVBP; Eukaryota.
DR   InParanoid; Q06355; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q06355; baseline.
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; Di-copper center containing domain from catechol oxidase; 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   PANTHER; PTHR11474:SF92; POLYPHENOL OXIDASE F, CHLOROPLASTIC; 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.
PE   2: Evidence at transcript level;
KW   Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW   Plastid; Reference proteome; Thioether bond; Thylakoid; Transit peptide.
FT   TRANSIT         <1..88
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           89..588
FT                   /note="Catechol oxidase B, chloroplastic"
FT                   /id="PRO_0000035917"
FT   BINDING         180
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         198
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         329
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         333
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         364
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   DISULFID        114..181
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        184..198
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   NON_TER         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
//