ID   TYRO_ASPOR              Reviewed;         539 AA.
AC   Q00234; Q2U3F5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 116.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1 {ECO:0000269|PubMed:7893753};
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=melO; ORFNames=AO090038000061;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=ATCC 22788 / RIB 128 / CBS 819.72 / IFO 30113 / JCM 2248;
RX   PubMed=7893753; DOI=10.1016/0167-4781(95)00011-5;
RA   Fujita Y., Uraga Y., Ichishima E.;
RT   "Molecular cloning and nucleotide sequence of the protyrosinase gene, melO,
RT   from Aspergillus oryzae and expression of the gene in yeast cells.";
RL   Biochim. Biophys. Acta 1261:151-154(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC       formation of pigments such as melanins and other polyphenolic
CC       compounds.
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         Evidence={ECO:0000269|PubMed:7893753};
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         Evidence={ECO:0000269|PubMed:7893753};
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   -!- ACTIVITY REGULATION: Activated by acidifying treatment at pH 3.0.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; D37929; BAA07149.1; -; Genomic_DNA.
DR   EMBL; AP007169; BAE63910.1; -; Genomic_DNA.
DR   PIR; S53529; S53529.
DR   RefSeq; XP_001825043.1; XM_001824991.2.
DR   AlphaFoldDB; Q00234; -.
DR   SMR; Q00234; -.
DR   STRING; 510516.Q00234; -.
DR   EnsemblFungi; BAE63910; BAE63910; AO090038000061.
DR   GeneID; 5997138; -.
DR   KEGG; aor:AO090038000061; -.
DR   VEuPathDB; FungiDB:AO090038000061; -.
DR   HOGENOM; CLU_026096_0_0_1; -.
DR   OMA; ANCQTHL; -.
DR   OrthoDB; 1908494at2759; -.
DR   Proteomes; UP000006564; Chromosome 6.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IDA:AspGD.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 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   Copper; Direct protein sequencing; Melanin biosynthesis; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Thioether bond.
FT   CHAIN           1..539
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000186733"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         84
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         93
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         290
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         294
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         333
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        82..84
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   539 AA;  60605 MW;  CD2ECD702A018E15 CRC64;
     MASVEPIKTF EIRQKGPVET KAERKSIRDL NEEELDKLIE AWRWIQDPAR TGEDSFFYLA
     GLHGEPFRGA GYNNSHWWGG YCHHGNILFP TWHRAYLMAV EKALRKACPD VSLPYWDESD
     DETAKKGIPL IFTQKEYKGK PNPLYSYTFS ERIVDRLAKF PDADYSKPQG YKTCRYPYSG
     LCGQDDIAIA QQHNNFLDAN FNQEQITGLL NSNVTSWLNL GQFTDIEGKQ VKADTRWKIR
     QCLLTEEYTV FSNTTSAQRW NDEQFHPLES GGKETEAKAT SLAVPLESPH NDMHLAIGGV
     QIPGFNVDQY AGANGDMGEN DTASFDPIFY FHHCFIDYLF WTWQTMHKKT DASQITILPE
     YPGTNSVDSQ GPTPGISGNT WLTLDTPLDP FRENGDKVTS NKLLTLKDLP YTYKAPTSGT
     GSVFNDVPRL NYPLSPPILR VSGINRASIA GSFALAISQT DHTGKAQVKG IESVLSRWHV
     QGCANCQTHL STTAFVPLFE LNEDDAKRKH ANNELAVHLH TRGNPGGQRV RNVTVGTMR
//