PPOB_SOLLC
ID PPOB_SOLLC Reviewed; 596 AA.
AC Q08304;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Polyphenol oxidase B, chloroplastic;
DE Short=PPO;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase;
DE Flags: Precursor;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry;
RX PubMed=8098228; DOI=10.1007/bf00023601;
RA Newman S.M., Eannetta N.T., Yu H., Prince J.P., de Vicente M.C.,
RA Tanksley S.D., Steffens J.C.;
RT "Organisation of the tomato polyphenol oxidase gene family.";
RL Plant Mol. Biol. 21:1035-1051(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; Z12834; CAA78296.1; -; Genomic_DNA.
DR PIR; S33540; S33540.
DR RefSeq; NP_001296326.1; NM_001309397.1.
DR AlphaFoldDB; Q08304; -.
DR SMR; Q08304; -.
DR STRING; 4081.Solyc08g074680.2.1; -.
DR PaxDb; Q08304; -.
DR GeneID; 101258774; -.
DR KEGG; sly:101258774; -.
DR eggNOG; ENOG502QVBP; Eukaryota.
DR OrthoDB; 881347at2759; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q08304; 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; 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 3: Inferred from homology;
KW Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW Plastid; Reference proteome; Thioether bond; Thylakoid; Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 88..596
FT /note="Polyphenol oxidase B, chloroplastic"
FT /id="PRO_0000035911"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 208
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 371
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 98..114
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 113..182
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 185..199
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 596 AA; 67227 MW; BD8553F7972FC7E8 CRC64;
MASVVCNSSS STTTTTLKTP FTSLGSTPKP SQLFLHGKRN KTFKVSCKVI NNNGNQDETN
SVDRRNVLLG LGGLYGVANA IPLAASATPI PSPDLKTCGR ATISDGPLVP YSCCPPPMPT
NFDTIPYYKF PSMTKLRIRT PAHAVDEEYI AKYNLAISRM RDLDKTEPLN PLGFKQQANI
HCAYCNGAYI IGGKELQVHN SWLFFPFHRW YLYFYERILG KLIDDPTFAL PYWNWDHPKG
MRLPPMFDRE GSSLYDERRN QQVRNGTVLD LGSFGDKVET TQLQLMSNNL TLMYRQMVTN
APCPLLFFGA PYVLGNNVEA PGTIETIPHI PVHIWAGTVR GSKFPNGDVS YGEDMGNFYS
AGLDPVFYCH HGNVDRMWNE WKAIGGKRRD ISEKDWLNSE FFFYDEHKNP YRVKVRDCLD
TKKMGYDYAP MPTPWRNFKP KSKASVGKVN TSTLPPANEV FPLAKMDKTI SFAINRPASS
RTQQEKNEQE EMLTFNNIRY DNRGYIRFDV FLNVDNNVNA NELDKAEFAG SYTSLPHVHR
AGENDHIAKV NFQLAITELL EDIGLEDEDT IAVTLVPKKG GEGISIENVE IKLVDC
