ID   TYRO_ASPFU              Reviewed;         630 AA.
AC   Q8J130; Q4WR60;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=tyr1; ORFNames=AFUA_1G17430;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46645 / NCPF 2109;
RA   Langfelder K., Glaser P., Brakhage A.A.;
RT   "Cloning of a tyrosinase gene of the human pathogenic fungus Aspergillus
RT   fumigatus.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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. {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:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; AJ293806; CAC82195.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL91072.1; -; Genomic_DNA.
DR   RefSeq; XP_753110.1; XM_748017.1.
DR   AlphaFoldDB; Q8J130; -.
DR   SMR; Q8J130; -.
DR   STRING; 746128.CADAFUBP00001648; -.
DR   GeneID; 3510142; -.
DR   KEGG; afm:AFUA_1G17430; -.
DR   VEuPathDB; FungiDB:Afu1g17430; -.
DR   eggNOG; ENOG502RYJI; Eukaryota.
DR   HOGENOM; CLU_013691_1_2_1; -.
DR   InParanoid; Q8J130; -.
DR   OrthoDB; 881347at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
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; IPR016216; Monophenol_mOase_fun.
DR   InterPro; IPR041640; Tyosinase_C.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   Pfam; PF18132; Tyosinase_C; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PIRSF; PIRSF000340; MPO_fungal; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Copper; Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Thioether bond.
FT   CHAIN           1..630
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000186732"
FT   BINDING         69
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         92
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         101
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         317
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         321
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         360
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        90..92
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CONFLICT        322..335
FT                   /note="Missing (in Ref. 2; EAL91072)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        600
FT                   /note="E -> D (in Ref. 1; CAC82195)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   630 AA;  73032 MW;  11A769BD9737BF35 CRC64;
     MSSNKPYVIK GIPVDAGQII PVRRDIDEWY EDTSRQSRIQ LSIFIWALRE FQSIDYKDRL
     SYFQIAGIHH FPLITWDEEE PPVPNKPGYC VHNNVTFPTW HRPYMLLFEQ RLFEIMETTI
     KETVPESHKQ EWRDAARQWR LPYWDFAKTS GPHATGPLSL PVLCGLANVV ILNPANPETP
     IELPNPVYKY RAPDLMGNLD KPFHIPPERI DPDKDDYYPW DKCQATTKYG LLKNNPHIQD
     AGQDVTKSNL ALNEHPWYRP NKAGFPPLQT LTYEVHRLLS FKFSSWGAFA STKWCNEENK
     PPASQQTRDI LSLEYIHNNV HNWVGGTDYL GDPSKPDLQG AGHMSSVPVA AFDPIFWLYH
     NNVDRLTAIW QVLNQDHWFD EPHPSDAKPD DPLKPFHVSK DKYFTSDDAR FWRKYGYDYD
     IVKKPGTNED RAPEEVKMKI NQLYGEPISR LHEGQPVEYD YVINVIYDRY ALDGIPYTIV
     FYLHLKDGSY KCLGGVYTFS TKLSDAQDTE RGGCDNCREQ KKAGVLASAQ IPLTYTLYER
     QEWHNLGKLL PVKETADIIR QHLCWKVVGV NNSILFDSEQ PMRGDPATWR SLDVTAAYSE
     IHYPVDRNYK YIDRGLPAYH NYLPIHLSPT