PPOE_SOLLC
ID PPOE_SOLLC Reviewed; 587 AA.
AC Q08307; Q41175;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Polyphenol oxidase E, 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Tiny tim;
RX PubMed=1633491; DOI=10.2307/3869567;
RA Shahar T., Hennig N., Gutfinger T., Hareven D., Lifschitz E.;
RT "The tomato 66.3-kD polyphenoloxidase gene: molecular identification and
RT developmental expression.";
RL Plant Cell 4:135-147(1992).
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; Z12837; CAA78299.1; -; Genomic_DNA.
DR EMBL; S40548; AAB22610.1; -; Genomic_DNA.
DR PIR; S33543; S33543.
DR AlphaFoldDB; Q08307; -.
DR SMR; Q08307; -.
DR STRING; 4081.Solyc08g074620.1.1; -.
DR PaxDb; Q08307; -.
DR PRIDE; Q08307; -.
DR eggNOG; ENOG502QVBP; Eukaryota.
DR BioCyc; MetaCyc:MON-16342; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q08307; 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 CHAIN 88..587
FT /note="Polyphenol oxidase E, chloroplastic"
FT /id="PRO_0000035914"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 328
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 332
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 363
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..180
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 183..197
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CONFLICT 311..315
FT /note="PLGSE -> LWVLN (in Ref. 2; AAB22610)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="C -> V (in Ref. 2; AAB22610)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="L -> V (in Ref. 2; AAB22610)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="V -> I (in Ref. 2; AAB22610)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="E -> G (in Ref. 2; AAB22610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 66237 MW; A796AA1DD6454E3D CRC64;
MSSSSSITTT LPLCTNKSLS SSFTTTNSSL LSKPSQLFLH GRRNQSFKVS CNANNVDKNP
DAVDRRNVLL GLGGLYGAAN LAPLATAAPI PPPDLKSCGT AHVKEGVDVI YSCCPPVPDD
IDSVPYYKFP SMTKLRIRPP AHAADEEYVA KYQLATSRMR ELDKDPFDPL GFKQQANIHC
AYCNGAYKVG GKELQVHFSW LFFPFHRWYL YFYERILGSL INDPTFALPY WNWDHPKGMR
IPPMFDREGS SLYDEKRNQN HRNGTIIDLG HFGKEVDTPQ LQIMTNNLTL MYRQMVTNAP
CPSQFFGAAY PLGSEPSPGQ GTIENIPHTP VHIWTGDKPR QKNGEDMGNF YSAGLDPIFY
CHHANVDRMW NEWKLIGGKR RDLTDKDWLN SEFFFYDENR NPYRVKVRDC LDSKKMGFDY
APMPTPWRNF KPIRKSSSGK VNTASIAPVS KVFPLAKLDR AISFSITRPA SSRTTQEKNE
QEEILTFNKI SYDDRNYVRF DVFLNVDKTV NADELDKAEF AGSYTSLPHV HGSNTNHVTS
LTFKLAITEL LEDIGLEDED TIAVTLVPKA GGEEVSIESV EIKLEDC
