TYRO_PHONA
ID TYRO_PHONA Reviewed; 625 AA.
AC A7BHQ9; A7BHR0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Tyrosinase {ECO:0000303|PubMed:17617709, ECO:0000312|EMBL:BAF74395.1};
DE EC=1.14.18.1;
DE Flags: Precursor;
GN Name=tyr1 {ECO:0000312|EMBL:BAF74395.1};
OS Pholiota nameko.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Strophariaceae; Pholiota.
OX NCBI_TaxID=61267;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF74395.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164; 175-195; 351-362
RP AND 384-387, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Fruiting body {ECO:0000269|PubMed:17617709};
RX PubMed=17617709; DOI=10.1271/bbb.70171;
RA Kawamura-Konishi Y., Tsuji M., Hatana S., Asanuma M., Kakuta D., Kawano T.,
RA Mukouyama E.B., Goto H., Suzuki H.;
RT "Purification, characterization, and molecular cloning of tyrosinase from
RT Pholiota nameko.";
RL Biosci. Biotechnol. Biochem. 71:1752-1760(2007).
CC -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC formation of pigments such as melanins and other polyphenolic
CC compounds. {ECO:0000250|UniProtKB:Q92396}.
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 Evidence={ECO:0000269|PubMed:17617709};
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 Evidence={ECO:0000269|PubMed:17617709};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:17617709};
CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:17617709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1930 uM for L-dopa {ECO:0000269|PubMed:17617709};
CC KM=119 uM for t-butylphenol {ECO:0000269|PubMed:17617709};
CC KM=30.6 uM for p-cresol {ECO:0000269|PubMed:17617709};
CC KM=163 uM for t-butylcatechol {ECO:0000269|PubMed:17617709};
CC KM=1240 uM for 3-(3,4-dihydroxyphenyl) propionic acid
CC {ECO:0000269|PubMed:17617709};
CC KM=122 uM for dopamine {ECO:0000269|PubMed:17617709};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17617709}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17617709}.
CC -!- MASS SPECTROMETRY: Mass=42424.39; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17617709};
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}.
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DR EMBL; AB275646; BAF74395.1; -; mRNA.
DR EMBL; AB275647; BAF74396.1; -; mRNA.
DR AlphaFoldDB; A7BHQ9; -.
DR SMR; A7BHQ9; -.
DR BRENDA; 1.14.18.1; 4764.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0004503; F:tyrosinase activity; IDA:UniProtKB.
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; IPR016216; Monophenol_mOase_fun.
DR InterPro; IPR041640; Tyosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000340; MPO_fungal; 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 CHAIN 1..387
FT /note="Tyrosinase"
FT /evidence="ECO:0000269|PubMed:17617709"
FT /id="PRO_0000352767"
FT PROPEP 388..625
FT /evidence="ECO:0000269|PubMed:17617709"
FT /id="PRO_0000352768"
FT BINDING 58
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 258
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 262
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 287
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CONFLICT 13
FT /note="I -> V (in Ref. 1; BAF74396)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="V -> A (in Ref. 1; BAF74396)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="G -> A (in Ref. 1; BAF74396)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="P -> S (in Ref. 1; BAF74396)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="S -> N (in Ref. 1; BAF74396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 67499 MW; 26E8AEFA285F871B CRC64;
MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS FFQIGGIHGL
PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL LYEQILHKHV QDIAATYTTS
DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI VSKKVTITGS NGHKVEVDNP LYHYKFHPID
SSFPRPYSEW PTTLRQPNSS RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS
NHTVGDGGST SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI
NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT KLGYTYPEFN
GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG SVASLAADVP LEKAPAPAPE
AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH AEPPVHVSAG GHPSPHGFYD WTARIEFKKY
EFGSSFSVLL FLGPVPEDPE QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL
TKYISEHAGL RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF
PVPGNRRHFH GITHGRVGGS RHAIV
