PPO3_AGABI
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 03-AUG-2022, entry version 33.
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; 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; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR041640; Tyosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 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
