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   20-JAN-2009, entry version 51.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=melO; ORFNames=AO090038000061;
OS   Aspergillus oryzae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 22788 / RIB 128 / CBS 819.72 / IFO 30113 / JCM 2248;
RX   MEDLINE=95200965; 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,
RT   melO, from Aspergillus oryzae and expression of the gene in yeast
RT   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.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., 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
CC       the formation of pigments such as melanins and other polyphenolic
CC       compounds.
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O(2) = L-dopa +
CC       dopaquinone + H(2)O.
CC   -!- COFACTOR: Binds 2 copper ions per subunit.
CC   -!- ENZYME 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.
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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; -.
DR   GeneID; 5997138; -.
DR   KEGG; aor:AO090038000061; -.
DR   BRENDA; 1.14.18.1; 2240.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:monophenol monooxygenase activity; IEA:EC.
DR   GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR008922; Di-copper_centre.
DR   InterPro; IPR016216; Monophenol_mOase_fun.
DR   InterPro; IPR002227; Tyrosinase.
DR   Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PIRSF; PIRSF000340; MPO_fungal; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Copper; Direct protein sequencing;
KW   Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Thioether bond.
FT   CHAIN         1    539       Tyrosinase.
FT                                /FTId=PRO_0000186733.
FT   METAL        63     63       Copper A (By similarity).
FT   METAL        84     84       Copper A (By similarity).
FT   METAL        93     93       Copper A (By similarity).
FT   METAL       290    290       Copper B (By similarity).
FT   METAL       294    294       Copper B (By similarity).
FT   METAL       333    333       Copper B (By similarity).
FT   CROSSLNK     82     84       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
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
//