PPO2_AGABI
ID PPO2_AGABI Reviewed; 556 AA.
AC O42713; Q12543;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Polyphenol oxidase 2;
DE Short=PPO2;
DE Short=Phenolase 2;
DE EC=1.14.18.1;
DE AltName: Full=Cresolase 2;
DE AltName: Full=Tyrosinase 2;
DE Flags: Precursor;
GN Name=PPO2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-556.
RC STRAIN=Horst U1;
RA Ebbelar C.E.M., Wichers H.J., Van Den Bosch T., Oyevaar J.I., Recourt K.;
RT "Characterization of a fruiting body-expressed gene encoding a putative
RT polyphenol oxidase of Agaricus bisporus.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=19711071; DOI=10.1007/s00253-009-2186-2;
RA Largeteau M.L., Latapy C., Minvielle N., Regnault-Roger C., Savoie J.M.;
RT "Expression of phenol oxidase and heat-shock genes during the development
RT of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium
RT fungicola.";
RL Appl. Microbiol. Biotechnol. 85:1499-1507(2010).
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 -!- DEVELOPMENTAL STAGE: Expressed during the fruiting body stage.
CC {ECO:0000269|PubMed:19711071}.
CC -!- PTM: The C-ter is probably cleaved after Gly-378 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61562.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ223816; CAA11562.1; -; mRNA.
DR EMBL; X89382; CAA61562.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; O42713; -.
DR SMR; O42713; -.
DR BindingDB; O42713; -.
DR ChEMBL; CHEMBL3318; -.
DR DrugCentral; O42713; -.
DR BRENDA; 1.14.18.1; 178.
DR SABIO-RK; O42713; -.
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..378
FT /note="Polyphenol oxidase 2"
FT /id="PRO_0000186731"
FT PROPEP 379..556
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000416863"
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 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 250
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 254
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT SITE 378..379
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CROSSLNK 79..81
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 556 AA; 63927 MW; DE10827A209895DA CRC64;
MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF FQLAGIHGLP
FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI LQGAAIEVAK KFTSNQTDWV
QAAQDLRQPY WDWGFELMPP DEVIKNEEVN ITNYDGKKIS VKNPILRYHF HPIDPSFKPY
GDFATWRTTV RNPDRNRRED IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD
QHANSLESVH DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW
VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS YPDFDKLVGG
TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT KEHKEDLKMY DWTIHVAFKK
FELKESFSLL FYFASDGGDY DQENCFVGSI NAFRGTAPET CANCQDNENL IQEGFIHLNH
YLARDLESFE PQDVHKFLKE KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH
TQARVVFDDV AVHVIN
