ID   TYRO_STRAT              Reviewed;         273 AA.
AC   P07524;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=melC2; Synonyms=mel;
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3932128; DOI=10.1016/0378-1119(85)90262-8;
RA   Bernan V., Filpula D., Herber W., Bibb M.J., Katz E.;
RT   "The nucleotide sequence of the tyrosinase gene from Streptomyces
RT   antibioticus and characterization of the gene product.";
RL   Gene 37:101-110(1985).
CC   -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC       formation of pigments such as melanins and other polyphenolic
CC       compounds.
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; M11582; AAA88571.1; -; Genomic_DNA.
DR   PIR; B23971; B23971.
DR   AlphaFoldDB; P07524; -.
DR   SMR; P07524; -.
DR   STRING; 1890.AFM16_02910; -.
DR   BRENDA; 1.14.18.1; 5974.
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; IPR002227; Tyrosinase_Cu-bd.
DR   Pfam; PF00264; Tyrosinase; 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.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..273
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000186737"
FT   BINDING         38
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         54
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         190
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         194
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         216
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   273 AA;  30739 MW;  FF22A3701AF975BA CRC64;
     MTVRKNQASL TAEEKRRFVA ALLELKRTGR YDAFVTTHNA FILGDTDNGE RTGHRSPSFL
     PWHRRFLLEF ERALQSVDAS VALPYWDWSA DRSTRSSLWA PDFLGGTGRS RDGQVMDGPF
     AASAGNWPIN VRVDGRTFLR RALGAGVSEL PTRAEVDSVL AMATYDMAPW NSGSDGFRNH
     LEGWRGVNLH NRVHVWVGGQ MATGVSPNDP VFWLHHAYID KLWAEWQRRH PSSPYLPGGG
     TPNVVDLNET MKPWNDTTPA ALLDHTRHYT FDV