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
//
