PPO1_AGABI
ID PPO1_AGABI Reviewed; 568 AA.
AC Q00024;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Polyphenol oxidase 1;
DE Short=PPO1;
DE Short=Phenolase 1;
DE EC=1.14.18.1;
DE AltName: Full=Cresolase 1;
DE AltName: Full=Tyrosinase 1;
DE Flags: Precursor;
GN Name=PPO1;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Horst U1;
RX PubMed=12743763; DOI=10.1007/s00253-002-1194-2;
RA Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G.,
RA Hoeberichts F., Mooibroek H., Soler-Rivas C.;
RT "Cloning, expression and characterisation of two tyrosinase cDNAs from
RT Agaricus bisporus.";
RL Appl. Microbiol. Biotechnol. 61:336-341(2003).
CC -!- FUNCTION: Copper-containing oxidase that catalyzes both the o-
CC hydroxylation of monophenols and the subsequent oxidation of the
CC resulting o-diphenols into reactive o-quinones, which evolve
CC spontaneously to produce intermediates, which associate in dark brown
CC pigments. Involved in the initial step of melanin synthesis. Melanins
CC constitute a mechanism of defense and resistance to stress such as UV
CC radiations, free radicals, gamma rays, dehydratation and extreme
CC temperatures, and contribute to the fungal cell-wall resistance against
CC hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also
CC involved in the formation and stability of spores (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:57924; EC=1.14.18.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC ChEBI:CHEBI:58315; EC=1.14.18.1;
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 -!- SUBUNIT: Heterotetramer. {ECO:0000250}.
CC -!- PTM: The C-ter is probably cleaved after Gly-382 since the mature
CC active protein is smaller than the protein encoded by the gene.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; X85113; CAA59432.1; -; mRNA.
DR PIR; S53017; S53017.
DR AlphaFoldDB; Q00024; -.
DR SMR; Q00024; -.
DR BindingDB; Q00024; -.
DR ChEMBL; CHEMBL3988582; -.
DR SABIO-RK; Q00024; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016216; Monophenol_mOase_fun.
DR InterPro; IPR041640; Tyosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000340; MPO_fungal; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Copper; Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW Thioether bond.
FT CHAIN 1..568
FT /note="Polyphenol oxidase 1"
FT /id="PRO_0000186740"
FT PROPEP 383..565
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000416862"
FT REGION 384..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 261
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT SITE 382..383
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CROSSLNK 83..85
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 568 AA; 63898 MW; F5CBADB73533685A CRC64;
MSHLLVSPLG GGVQPRLEIN NFVKNDRQFS LYVQALDRMY ATPQNETASY FQVAGVHGYP
LIPFDDAVGP TEFSPFDQWT GYCTHGSTLF PTWHRPYVLI LEQILSGHAQ QIADTYTVNK
SEWKKAATEF RHPYWDWASN SVPPPEVISL PKVTITTPNG QKTSVANPLM RYTFNSVNDG
GFYGPYNQWD TTLRQPDSTG VNAKDNVNRL KSVLKNAQAS LTRATYDMFN RVTTWPHFSS
HTPASGGSTS NSIEAIHDNI HVLVGGNGHM SDPSVAPFDP IFFLHHANVD RLIALWSAIR
YDVWTSPGDA QFGTYTLRYK QSVDESTDLA PWWKTQNEYW KSNELRSTES LGYTYPEFVG
LDMYNKDAVN KTISRKVAQL YGPQRGGQRS LVEDLSNSHA RRSQRPAKRS RLGQLLKGLF
SDWSAQIKFN RHEVGQSFSV CLFLGNVPED PREWLVSPNL VGARHAFVRS VKTDHVAEEI
GFIPINQWIA EHTGLPSFAV DLVKPLLAQG LQWRVLLADG TPAELDSLEV TILEVPSELT
DDEPNPRSRP PRYHKDITHG KRGGCREA
