ID   TYRO_STRLN              Reviewed;         273 AA.
AC   P55023;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-JAN-2009, entry version 43.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=melC2; Synonyms=mel;
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=78-11;
RA   Zhang H.Z., Piepersberg W.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the tyrosinase family.
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DR   EMBL; X95703; CAA65000.1; -; Genomic_DNA.
DR   HSSP; O61363; 1JS8.
DR   SMR; P55023; 2-271.
DR   BRENDA; 1.14.18.1; 289191.
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; IPR002227; Tyrosinase.
DR   Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Copper; Melanin biosynthesis; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    273       Tyrosinase.
FT                                /FTId=PRO_0000186739.
FT   METAL        37     37       Copper A (By similarity).
FT   METAL        53     53       Copper A (By similarity).
FT   METAL        62     62       Copper A (By similarity).
FT   METAL       189    189       Copper B (By similarity).
FT   METAL       193    193       Copper B (By similarity).
FT   METAL       215    215       Copper B (By similarity).
SQ   SEQUENCE   273 AA;  30854 MW;  E9D8616C99DD4DB9 CRC64;
     MTVRKNQATL TADEKRRFVT AVLSSSAARY DTFVTTHNEF IVADTDNGER TGHRSPSFLP
     WHRRFLLEFE RALQSVDASV ALPYWDWSTD RSARSSLWAP DFLGGTGRSR NGRVTDGPFR
     AATGVWPITV RLDGRTYLRR ALGGAGRELP TRAEVDSVLS IPTYDMAPWN SASDGFRNHL
     EGWRGVNLHN RVHVWVGGQM ATGVSPNDPV FWLHHAYIDK LWAQWQRRHR TPAYVPAAGT
     PDVVDLDETM KPWHDSSPAD LLDHTGHYTF DTD
//