PPO_MALDO
ID PPO_MALDO Reviewed; 593 AA.
AC P43309;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Polyphenol oxidase, chloroplastic;
DE Short=PPO;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase;
DE Flags: Precursor;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=7888632; DOI=10.1007/bf00020197;
RA Boss P.K., Gardner R.C., Janssen B.-J., Ross G.S.;
RT "An apple polyphenol oxidase cDNA is up-regulated in wounded tissues.";
RL Plant Mol. Biol. 27:429-433(1995).
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; L29450; AAA69902.1; -; mRNA.
DR PIR; S52984; S52984.
DR RefSeq; NP_001306190.1; NM_001319261.1.
DR PDB; 6ELS; X-ray; 1.35 A; A=90-593.
DR PDB; 6ELT; X-ray; 1.35 A; A=458-593.
DR PDB; 6ELV; X-ray; 1.05 A; A=451-593.
DR PDBsum; 6ELS; -.
DR PDBsum; 6ELT; -.
DR PDBsum; 6ELV; -.
DR AlphaFoldDB; P43309; -.
DR SMR; P43309; -.
DR STRING; 3750.XP_008383785.1; -.
DR EnsemblPlants; mRNA:MD10G0254000; CDS:MD10G0254000.1; MD10G0254000.
DR GeneID; 103446446; -.
DR Gramene; mRNA:MD10G0254000; CDS:MD10G0254000.1; MD10G0254000.
DR KEGG; mdm:103446446; -.
DR OrthoDB; 881347at2759; -.
DR BRENDA; 1.14.18.1; 3164.
DR SABIO-RK; P43309; -.
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; Thioether bond; Thylakoid; Transit peptide.
FT TRANSIT 1..89
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 90..593
FT /note="Polyphenol oxidase, chloroplastic"
FT /id="PRO_0000035916"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 205
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 327
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 361
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 100..115
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 114..176
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 179..196
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 201..219
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:6ELS"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:6ELS"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:6ELS"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6ELS"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:6ELS"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6ELS"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:6ELV"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:6ELV"
FT TURN 487..492
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 496..505
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 510..518
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 546..555
FT /evidence="ECO:0007829|PDB:6ELV"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 569..580
FT /evidence="ECO:0007829|PDB:6ELV"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:6ELV"
SQ SEQUENCE 593 AA; 65721 MW; 545296ADB9DD13B9 CRC64;
MTSLSPPVVT TPTVPNPATK PLSPFSQNNS QVSLLTKPKR SFARKVSCKA TNNDQNDQAQ
SKLDRRNVLL GLGGLYGVAG MGTDPFAFAK PIAPPDVSKC GPADLPQGAV PTNCCPPPST
KIIDFKLPAP AKLRIRPPAH AVDQAYRDKY YKAMELMKAL PDDDPRSFKQ QAAVHCAYCD
GAYDQVGFPE LELQIHNSWL FFPFHRYYLY FFEKILGKLI NDPTFALPFW NWDSPAGMPL
PAIYADPKSP LYDKLRSANH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN
AKLFFGNPYR AGDEPDPGGG SIEGTPHAPV HLWTGDNTQP NFEDMGNFYS AGRDPIFFAH
HSNVDRMWSI WKTLGGKRTD LTDSDWLDSG FLFYNENAEL VRVKVRDCLE TKNLGYVYQD
VDIPWLSSKP TPRRAKVALS KVAKKLGVAH AAVASSSKVV AGTEFPISLG SKISTVVKRP
KQKKRSKKAK EDEEEILVIE GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH
SHKHKKKMNT ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS
