ID   TYRO_AGABI     STANDARD;      PRT;   556 AA.
AC   O42713;
DT   30-MAY-2000 (Rel. 39, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase) (Phenolase)
DE   (Monophenol oxidase) (Cresolase).
GN   Name=ppo2;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Horst U1;
RX   MEDLINE=22627160; PubMed=12743763; DOI=10.1007/s00253-002-1194-2;
RA   Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G.,
RA   Hoeberichts F., Mooibroek H., Soler-Rivas C.;
RT   "Cloning, expression and characterisation of two tyrosinase cDNAs from
RT   Agaricus bisporus.";
RL   Appl. Microbiol. Biotechnol. 61:336-341(2003).
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 (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed during the fruiting body stage.
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
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CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AJ223816; CAA11562.1; -.
DR   InterPro; IPR008922; Di-copper_centre.
DR   InterPro; IPR002227; Tyrosinase.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
KW   Copper; Melanin biosynthesis; Monooxygenase; Oxidoreductase.
FT   METAL        57     57       Copper A (By similarity).
FT   METAL        81     81       Copper A (By similarity).
FT   METAL        90     90       Copper A (By similarity).
FT   METAL       250    250       Copper B (By similarity).
FT   METAL       254    254       Copper B (By similarity).
FT   METAL       282    282       Copper B (By similarity).
SQ   SEQUENCE   556 AA;  63927 MW;  DE10827A209895DA CRC64;
     MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF FQLAGIHGLP
     FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI LQGAAIEVAK KFTSNQTDWV
     QAAQDLRQPY WDWGFELMPP DEVIKNEEVN ITNYDGKKIS VKNPILRYHF HPIDPSFKPY
     GDFATWRTTV RNPDRNRRED IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD
     QHANSLESVH DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW
     VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS YPDFDKLVGG
     TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT KEHKEDLKMY DWTIHVAFKK
     FELKESFSLL FYFASDGGDY DQENCFVGSI NAFRGTAPET CANCQDNENL IQEGFIHLNH
     YLARDLESFE PQDVHKFLKE KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH
     TQARVVFDDV AVHVIN
//