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 13-SEP-2023, entry version 37. 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; Agaricineae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 2.60.310.20; -; 1. 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; IPR016216; Monophenol_mOase_fun. DR InterPro; IPR041640; Tyrosinase_C. DR InterPro; IPR002227; Tyrosinase_Cu-bd. DR PANTHER; PTHR11474:SF76; TYROSINASE; 1. DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1. DR Pfam; PF18132; Tyosinase_C; 1. DR Pfam; PF00264; Tyrosinase; 1. DR PIRSF; PIRSF000340; MPO_fungal; 1. DR PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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 //