PPOA_SOLLC
ID PPOA_SOLLC Reviewed; 630 AA.
AC Q08303;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Polyphenol oxidase A, 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; Z12833; CAA78295.1; -; Genomic_DNA.
DR PIR; S33539; S33539.
DR PDB; 6HQI; X-ray; 1.85 A; A=88-591.
DR PDB; 6HQJ; X-ray; 1.80 A; A=88-591.
DR PDBsum; 6HQI; -.
DR PDBsum; 6HQJ; -.
DR AlphaFoldDB; Q08303; -.
DR SMR; Q08303; -.
DR BioCyc; MetaCyc:MON-16344; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q08303; 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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Plastid; Reference proteome; Thioether bond; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 88..630
FT /note="Polyphenol oxidase A, chloroplastic"
FT /id="PRO_0000035910"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 370
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"
FT DISULFID 113..181
FT /evidence="ECO:0000250"
FT CROSSLNK 184..198
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 146..165
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 203..221
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:6HQJ"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:6HQJ"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6HQJ"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 365..381
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 482..487
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 488..499
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 527..533
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:6HQJ"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 568..579
FT /evidence="ECO:0007829|PDB:6HQJ"
FT STRAND 582..591
FT /evidence="ECO:0007829|PDB:6HQJ"
SQ SEQUENCE 630 AA; 70616 MW; 821F3297879326F1 CRC64;
MASLCSNSSS TSLKTPFTSS TTCLSSTPTA SQLFLHGKRN KTFKVSCKVT NTNGNQDETN
SVDRRNVLLG LGGLYGVANA IPLAASAAPT PPPDLSSCNK PKINATTEVP YFCCAPKPDD
MSKVPYYKFP SVTKLRIRPP AHALDEAYIA KYNLAISRMK DLDKTQPDNP IGFKQQANIH
CAYCNGGYSI DGKVLQVHNS WLFFPFHRWY LYFYERILGS LIDDPTFGLP FWNWDHPKGM
RFPPMFDVPG TALYDERRGD QIHNGNGIDL GYFGDQVETT QLQLMTNNLT LMYRQLVTNS
PCPLMSLVDL TLFGSTVEDA GTVENIPHSP VHIWVGTRRG SVLPVGKISN GEDMGNFYSA
GLDPLFYCHH SNVDRMWNEW KATGGKRTDI QNKDWLNSEF FFYDENGNPF KVRVRDCLDT
KKMGYDYHAT ATPWRNFKPK TKASAGKVNT GSIPPESQVF PLAKLDKAIS FSINRPASSR
TQQEKNAQEE VLTFNAIKYD NRDYIRFDVF LNVDNNVNAN ELDKAEFAGS YTSLPHVHRV
GDPKHTATAT LRLAITELLE DIGLEDEDTI AVTLVPKKGD ISIGGVEIKL AIVKLVCVVN
LLTLQLNKDR FCYDSVFVCW FVCLFFNFHV
