ID PPO3_AGABI Reviewed; 576 AA. AC C7FF04; D5LK97; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 1. DT 13-SEP-2023, entry version 36. DE RecName: Full=Polyphenol oxidase 3; DE Short=PPO3; DE Short=Phenolase 3; DE EC=1.14.18.1; DE AltName: Full=Cresolase; DE AltName: Full=Tyrosinase 3; DE Flags: Precursor; GN Name=PPO3; 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. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-392 IN COMPLEX WITH SUBSTRATE, RP COFACTOR, AND THIOESTER BOND. RX PubMed=21598903; DOI=10.1021/bi200395t; RA Ismaya W.T., Rozeboom H.J., Weijn A., Mes J.J., Fusetti F., Wichers H.J., RA Dijkstra B.W.; RT "Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of RT the tetramer subunits and interaction with tropolone."; RL Biochemistry 50:5477-5486(2011). 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:0000269|PubMed:21598903}; CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:21598903}; CC -!- SUBUNIT: Tetramer composed of two subunits of PPO3 (H subunits) and two CC subunits of the as yet uncharacterized product of ORF239342 (L CC subunits). {ECO:0000269|PubMed:21598903}. CC -!- PTM: The C-ter is probably cleaved after Gly-392 since the mature CC active protein is smaller than the protein encoded by the gene. 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; GQ354801; ACU29457.1; -; mRNA. DR EMBL; GU936494; ADE67053.1; -; Genomic_DNA. DR PDB; 2Y9W; X-ray; 2.30 A; A/B=2-392. DR PDB; 2Y9X; X-ray; 2.78 A; A/B/C/D=2-392. DR PDBsum; 2Y9W; -. DR PDBsum; 2Y9X; -. DR AlphaFoldDB; C7FF04; -. DR SMR; C7FF04; -. DR BRENDA; 1.14.18.1; 178. DR EvolutionaryTrace; C7FF04; -. 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; 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 PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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..392 FT /note="Polyphenol oxidase 3" FT /id="PRO_0000416864" FT PROPEP 393..576 FT /note="Removed in mature form" FT /evidence="ECO:0000305" FT /id="PRO_0000416865" FT BINDING 61 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 85 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 94 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 259 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 263 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21598903" FT BINDING 296 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21598903" FT SITE 392..393 FT /note="Cleavage" FT /evidence="ECO:0000305" FT CROSSLNK 83..85 FT /note="2'-(S-cysteinyl)-histidine (Cys-His)" FT /evidence="ECO:0000269|PubMed:21598903" FT CONFLICT 106 FT /note="W -> C (in Ref. 2; ADE67053)" FT /evidence="ECO:0000305" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 23..26 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 30..45 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 54..59 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 90..113 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 121..130 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:2Y9W" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:2Y9X" FT HELIX 210..233 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 238..242 FT /evidence="ECO:0007829|PDB:2Y9W" FT TURN 245..249 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 255..267 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:2Y9W" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 291..309 FT /evidence="ECO:0007829|PDB:2Y9W" FT TURN 310..312 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:2Y9X" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:2Y9X" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:2Y9X" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 352..355 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:2Y9W" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:2Y9X" FT HELIX 366..371 FT /evidence="ECO:0007829|PDB:2Y9W" FT HELIX 376..391 FT /evidence="ECO:0007829|PDB:2Y9W" SQ SEQUENCE 576 AA; 66267 MW; A4ED6B3B762DCB26 CRC64; MSDKKSLMPL VGIPGEIKNR LNILDFVKND KFFTLYVRAL QVLQARDQSD YSSFFQLGGI HGLPYTEWAK AQPQLHLYKA NYCTHGTVLF PTWHRAYEST WEQTLWEAAG TVAQRFTTSD QAEWIQAAKD LRQPFWDWGY WPNDPDFIGL PDQVIRDKQV EITDYNGTKI EVENPILHYK FHPIEPTFEG DFAQWQTTMR YPDVQKQENI EGMIAGIKAA APGFREWTFN MLTKNYTWEL FSNHGAVVGA HANSLEMVHN TVHFLIGRDP TLDPLVPGHM GSVPHAAFDP IFWMHHCNVD RLLALWQTMN YDVYVSEGMN REATMGLIPG QVLTEDSPLE PFYTKNQDPW QSDDLEDWET LGFSYPDFDP VKGKSKEEKS VYINDWVHKH YGFVTTQTEN PALRLLSSFQ RAKSDHETQY ALYDWVIHAT FRYYELNNSF SIIFYFDEGE GCTLESIIGT VDAFRGTTSE NCANCARSQD LIAEGFVHLN YYIGCDIGQH ADHEDDAVPL YEPTRVKEYL KKRKIGCKVV SAEGELTSLV VEIKGAPYYL PVGEARPKLD HEKPIVILDD IIHRVN //