TYRO_STRGA
ID TYRO_STRGA Reviewed; 274 AA.
AC P06845;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tyrosinase;
DE EC=1.14.18.1;
DE AltName: Full=Monophenol monooxygenase;
GN Name=melC2; Synonyms=mel;
OS Streptomyces glaucescens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=3002431; DOI=10.1021/bi00343a003;
RA Huber M., Hintermann G., Lerch K.;
RT "Primary structure of tyrosinase from Streptomyces glaucescens.";
RL Biochemistry 24:6038-6044(1985).
RN [2]
RP COPPER-LIGANDS, MUTAGENESIS, AND COFACTOR.
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=2846043; DOI=10.1021/bi00415a032;
RA Huber M., Lerch K.;
RT "Identification of two histidines as copper ligands in Streptomyces
RT glaucescens tyrosinase.";
RL Biochemistry 27:5610-5615(1988).
RN [3]
RP COPPER-LIGANDS, MUTAGENESIS, AND COFACTOR.
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=1901488; DOI=10.1042/bj2740707;
RA Jackman M.P., Hajnal A., Lerch K.;
RT "Albino mutants of Streptomyces glaucescens tyrosinase.";
RL Biochem. J. 274:707-713(1991).
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:0000269|PubMed:1901488, ECO:0000269|PubMed:2846043};
CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:1901488,
CC ECO:0000269|PubMed:2846043};
CC -!- MISCELLANEOUS: The extra- and intra-cellular tyrosinases are identical.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; M11302; AAA26834.1; -; Genomic_DNA.
DR PIR; A24089; A24089.
DR RefSeq; WP_043498008.1; NZ_CP009438.1.
DR AlphaFoldDB; P06845; -.
DR SMR; P06845; -.
DR STRING; 1907.SGLAU_02720; -.
DR eggNOG; COG2304; Bacteria.
DR OMA; SLWAPDF; -.
DR OrthoDB; 446922at2; -.
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 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Melanin biosynthesis; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..274
FT /note="Tyrosinase"
FT /id="PRO_0000186738"
FT BINDING 38
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT BINDING 54
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT BINDING 63
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT BINDING 190
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT BINDING 216
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 38
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 54
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 63
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 190
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 191
FT /note="N->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 194
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT MUTAGEN 216
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1901488,
FT ECO:0000269|PubMed:2846043"
FT CONFLICT 216
FT /note="H -> N (in Ref. 1; AAA26834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30874 MW; 0FDC67DC2739AA79 CRC64;
MTVRKNQATL TADEKRRFVA AVLELKRSGR YDEFVTTHNA FIIGDTDAGE RTGHRSPSFL
PWHRRYLLEF ERALQSVDAS VALPYWDWSA DRTARASLWA PDFLGGTGRS LDGRVMDGPF
AASAGNWPIN VRVDGRAYLR RSLGTAVREL PTRAEVESVL GMATYDTAPW NSASDGFRNH
LEGWRGVNLH NRVHVWVGGQ MATGMSPNDP VFWLHHAYVD KLWAEWQRRH PGSGYLPAAG
TPDVVDLNDR MKPWNDTSPA DLLDHTAHYT FDTD
