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   20-JAN-2009, entry version 34.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=tyr1; ORFNames=AFUA_1G17430;
OS   Aspergillus fumigatus (Sartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5085;
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
RT   Aspergillus fumigatus.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   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.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., 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
CC       the formation of pigments such as melanins and other polyphenolic
CC       compounds (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O(2) = L-dopa +
CC       dopaquinone + H(2)O.
CC   -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
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DR   EMBL; AJ293806; CAC82195.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL91072.1; -; Genomic_DNA.
DR   RefSeq; XP_753110.1; -.
DR   GeneID; 3510142; -.
DR   KEGG; afm:AFUA_1G17430; -.
DR   HOGENOM; Q8J130; -.
DR   BRENDA; 1.14.18.1; 18841.
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   3: Inferred from homology;
KW   Complete proteome; Copper; Melanin biosynthesis; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Thioether bond.
FT   CHAIN         1    630       Tyrosinase.
FT                                /FTId=PRO_0000186732.
FT   METAL        69     69       Copper A (By similarity).
FT   METAL        92     92       Copper A (By similarity).
FT   METAL       101    101       Copper A (By similarity).
FT   METAL       317    317       Copper B (By similarity).
FT   METAL       321    321       Copper B (By similarity).
FT   METAL       360    360       Copper B (By similarity).
FT   CROSSLNK     90     92       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
FT   CONFLICT    322    335       Missing (in Ref. 2; EAL91072).
FT   CONFLICT    600    600       E -> D (in Ref. 1; CAC82195).
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
//