ID   PPO1_AGABI     STANDARD;      PRT;   568 AA.
AC   Q00024;
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   Polyphenol oxidase (EC 1.10.3.1) (PPO) (Catechol oxidase).
GN   Name=ppo1;
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: Catalyzes the oxidation of mono- and o-diphenols to o-
CC       diquinones.
CC   -!- CATALYTIC ACTIVITY: 2 catechol + O(2) = 2 1,2-benzoquinone + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
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
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DR   EMBL; X85113; CAA59432.1; -.
DR   PIR; S53017; S53017.
DR   InterPro; IPR008922; Di-copper_centre.
DR   InterPro; IPR008958; Transglut_C.
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; Monooxygenase; Oxidoreductase; Thioether bond.
FT   METAL        57     57       Copper A (By similarity).
FT   METAL        85     85       Copper A (By similarity).
FT   METAL        94     94       Copper A (By similarity).
FT   METAL       257    257       Copper B (By similarity).
FT   METAL       261    261       Copper B (By similarity).
FT   METAL       286    286       Copper B (By similarity).
FT   CROSSLNK     83     85       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
SQ   SEQUENCE   568 AA;  63898 MW;  F5CBADB73533685A CRC64;
     MSHLLVSPLG GGVQPRLEIN NFVKNDRQFS LYVQALDRMY ATPQNETASY FQVAGVHGYP
     LIPFDDAVGP TEFSPFDQWT GYCTHGSTLF PTWHRPYVLI LEQILSGHAQ QIADTYTVNK
     SEWKKAATEF RHPYWDWASN SVPPPEVISL PKVTITTPNG QKTSVANPLM RYTFNSVNDG
     GFYGPYNQWD TTLRQPDSTG VNAKDNVNRL KSVLKNAQAS LTRATYDMFN RVTTWPHFSS
     HTPASGGSTS NSIEAIHDNI HVLVGGNGHM SDPSVAPFDP IFFLHHANVD RLIALWSAIR
     YDVWTSPGDA QFGTYTLRYK QSVDESTDLA PWWKTQNEYW KSNELRSTES LGYTYPEFVG
     LDMYNKDAVN KTISRKVAQL YGPQRGGQRS LVEDLSNSHA RRSQRPAKRS RLGQLLKGLF
     SDWSAQIKFN RHEVGQSFSV CLFLGNVPED PREWLVSPNL VGARHAFVRS VKTDHVAEEI
     GFIPINQWIA EHTGLPSFAV DLVKPLLAQG LQWRVLLADG TPAELDSLEV TILEVPSELT
     DDEPNPRSRP PRYHKDITHG KRGGCREA
//