PPO_VICFA
ID PPO_VICFA Reviewed; 606 AA.
AC Q06215;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Polyphenol oxidase A1, chloroplastic;
DE Short=PPO;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase;
DE Flags: Precursor;
OS Vicia faba (Broad bean) (Faba vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=1391768; DOI=10.1007/bf00014492;
RA Cary J.W., Lax A.R., Flurkey W.H.;
RT "Cloning and characterization of cDNAs coding for Vicia faba polyphenol
RT oxidase.";
RL Plant Mol. Biol. 20:245-253(1992).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 93-119.
RC TISSUE=Leaf;
RX PubMed=16667057; DOI=10.1104/pp.91.2.481;
RA Flurkey W.H.;
RT "Polypeptide composition and amino-terminal sequence of broad bean
RT polyphenol oxidase.";
RL Plant Physiol. 91:481-483(1989).
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; Z11702; CAA77764.1; -; mRNA.
DR PIR; S24758; S24758.
DR AlphaFoldDB; Q06215; -.
DR SMR; Q06215; -.
DR PRIDE; Q06215; -.
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 Chloroplast; Copper; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Plastid; Thioether bond; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..92
FT /note="Chloroplast"
FT CHAIN 93..606
FT /note="Polyphenol oxidase A1, chloroplastic"
FT /id="PRO_0000035919"
FT REGION 32..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
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 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
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 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 367
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 103..121
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 120..182
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 185..202
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 606 AA; 68541 MW; FC539F9F041B503C CRC64;
MTSISALSFI STINVSSNSK ISHSSVYPFL QKQHQSSKLR KPKRQVTCSS NNNQNNPKEE
QELSNIVGHR RNVLIGLGGI YGTLATNPSA LASPISPPDL SKCVPPSDLP SGTTPPNINC
CPPYSTKITD FKFPSNQPLR VRQAAHLVDN EFLEKYKKAT ELMKALPSND PRNFTQQANI
HCAYCDGAYS QIGFPDLKLQ VHGSWLFFPF HRWYLYFYER ILGSLINDPT FALPFWNYDA
PDGMQLPTIY ADKASPLYDE LRNASHQPPT LIDLNFCDIG SDIDRNELIK TNLSIMYRQV
YSNGKTSRLF LGNPYRAGDA EPQGAGSIEN VPHAPVHTWT GDNTQTNIED MGIFYSAARD
PIFYSHHSNV DRLWYIWKTL GGKKHDFTDK DWLESGFLFY DENKNLVRVN VKDSLDIDKL
GYAYQDVPIP WEKAKPVPRR TKVQKLVEVE VNDGNLRKSP TIFLVRQQSP RKYVTFPLVL
NNKVSAIVKR PKKLRSKKEK EEEEEVLVIE GIEFYMNIAI KFDVYINDED DKVGAGNTEF
AGSFVNIPHS AHGHKNKKII TSLRLGITDL LEDLHVEGDD NIVVTLVPKC GSGQVKINNV
EIVFED
