ID O24057_MALDO Unreviewed; 593 AA.
AC O24057;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:BAA21677.1};
DE EC=1.10.3.1 {ECO:0000313|EMBL:BAA21677.1};
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 {ECO:0000313|EMBL:BAA21677.1};
RN [1] {ECO:0000313|EMBL:BAA21677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fuji {ECO:0000313|EMBL:BAA21677.1};
RX PubMed=9532795; DOI=10.1271/bbb.62.358;
RA Haruta M., Murata M., Hiraide A., Kadokura H., Yamasaki M., Sakuta M.,
RA Shimizu S., Homma S.;
RT "Cloning genomic DNA encoding apple polyphenol oxidase and comparison of
RT the gene product in Escherichia coli and in apple.";
RL Biosci. Biotechnol. Biochem. 62:358-362(1998).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR000290-1};
CC Note=Binds 2 copper ions per subunit. {ECO:0000256|PIRSR:PIRSR000290-
CC 1};
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; D87670; BAA21677.1; -; Genomic_DNA.
DR AlphaFoldDB; O24057; -.
DR SMR; O24057; -.
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; Di-copper center containing domain from catechol oxidase; 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 PANTHER; PTHR11474:SF138; OS04G0624500 PROTEIN; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
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; Di-copper centre-containing domain; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR000290-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000290-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000290-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAA21677.1};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 354..365
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
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:0000256|PIRSR:PIRSR000290-1"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 205
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 327
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 361
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 100..115
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 114..176
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 179..196
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 593 AA; 65744 MW; A8DB902D184F29E5 CRC64;
MTSLSPPVVT TPTVPNPDTK PLSPFSQNNS QVSLLTKPKR SFGRKVSCKD TNNDEIDQAQ
SKLERRNVLL GLGGLYGVGG MDTDPRGWGK AIAPPDVSKC GPADLPQGGV PTICCPPRST
KIIDFKLPAP AKLRIRPPAH AGDQAYRDKH YKAMELMKAL PDDDPRSFKQ QGAVHCAYCD
GAYDQVGFPE LELQIHNSWL FFPLHRYYLY FFEKILGKLI NDPTFAGPFW NWDSPAGMPL
PAIYADPKSP LYDKLRSAQH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN
AKLFFGNPYR AGDEPDPGGG SIEGTPHAPV HLWTGDNTQP NFEDMGNFYS AGRDPIFFAH
HSNVDRMWSI WKTLGGKRAD LTDSDWLDSG FLFYNENAEL VRVKVRDCLE TKNLGYVYQD
VDIPWLSSKP TPRRAKVALS KIAKKLGVAH AAVASSSKVV AGTEFPINLG SKISTVVKRP
KQKKRSKKAK EDEEEILVIE GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH
SHKHKKKMNT ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS
//
