PPO4_AGABI
ID PPO4_AGABI Reviewed; 611 AA.
AC C7FF05;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Polyphenol oxidase 4;
DE Short=PPO4;
DE Short=Phenolase 4;
DE EC=1.14.18.1;
DE AltName: Full=Cresolase;
DE AltName: Full=Tyrosinase 4;
DE Flags: Precursor;
GN Name=PPO4;
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].
RX PubMed=20676921; DOI=10.1007/s10529-010-0329-2;
RA Wu J., Chen H., Gao J., Liu X., Cheng W., Ma X.;
RT "Cloning, characterization and expression of two new polyphenol oxidase
RT cDNAs from Agaricus bisporus.";
RL Biotechnol. Lett. 32:1439-1447(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=As2796;
RA Li N.Y., Cai W.M., Liu C.Y., Ran F.L.;
RT "Molecular cloning and characterization of two polyphenoloxidase genes from
RT the mushrooms Agaricus bisporus.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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-379 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; GQ354802; ACU29458.1; -; mRNA.
DR EMBL; GU936493; ADE67052.1; -; Genomic_DNA.
DR PDB; 5M6B; X-ray; 3.25 A; A/B/C/D=1-565.
DR PDBsum; 5M6B; -.
DR AlphaFoldDB; C7FF05; -.
DR SMR; C7FF05; -.
DR BRENDA; 1.14.18.1; 178.
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 1: Evidence at protein level;
KW 3D-structure; Copper; Melanin biosynthesis; Metal-binding; Monooxygenase;
KW Oxidoreductase; Thioether bond.
FT CHAIN 1..379
FT /note="Polyphenol oxidase 4"
FT /id="PRO_0000416866"
FT PROPEP 380..611
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000416867"
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 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 91
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 251
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 255
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT SITE 379..380
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CROSSLNK 80..82
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 87..110
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 202..225
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5M6B"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 408..420
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:5M6B"
FT HELIX 492..501
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 504..514
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 521..531
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:5M6B"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:5M6B"
SQ SEQUENCE 611 AA; 68318 MW; D9667D24204E614B CRC64;
MSLLATVGPT GGVKNRLDIV DFVRDEKFFT LYVRALQAIQ DKDQADYSSF FQLSGIHGLP
FTPWAKPKDT PTVPYESGYC THSQVLFPTW HRVYVSIYEQ VLQEAAKGIA KKFTVHKKEW
VQAAEDLRQP YWDTGFALVP PDEIIKLEQV KITNYDGTKI TVRNPILRYS FHPIDPSFSG
YPNFDTWRTT VRNPDADKKE NIPALIAKLD LEADSTREKT YNMLKFNANW EAFSNHGEFD
DTHANSLEAV HDDIHGFVGR GAIRGHMTHA LFAAFDPIFW LHHSNVDRHL SLWQALYPGV
WVTQGPEREG SMGFAPGTEL NKDSALEPFY ETEDKPWTSV PLTDTALLNY SYPDFDKVKG
GTPDLVRDYI NDHIDRRYGI KKSEGGKNPA LDLLSDFKGV THDHNEDLKM FDWTIQASWK
KFELDDSFAI IFYFAADGST NVTKENYIGS INIFRGTTPT NCANCRTQDN LVQEGFVHLD
RFIARDLDTF DPQAVHRYLK EKKLSYKVVA DDHSVTLKSL RIRVQGRPLH LPPGVSFPRL
DKNIPIVNFD DVLDLVTGVV NIGLTAVGAT AGVAIGVVGA TAGTAIGVAG AATDAVTNIA
KGGLGALGRI F
