ID   TYRO_PODAS              Reviewed;         574 AA.
AC   Q92396;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=TYR;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=S1;
RA   Marbach K., Stahl U.;
RT   "Molecular and functional characterization of the tyrosinase gene of the
RT   filamentous fungus Podospora anserina.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U66808; AAB07516.1; -; mRNA.
DR   EMBL; U66807; AAB07484.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92396; -.
DR   SMR; Q92396; -.
DR   PRIDE; Q92396; -.
DR   VEuPathDB; FungiDB:PODANS_1_5740; -.
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; 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   2: Evidence at transcript level;
KW   Copper; Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Thioether bond.
FT   CHAIN           1..574
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000186734"
FT   BINDING         67
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         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         275
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         279
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         304
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CROSSLNK        93..95
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   574 AA;  64181 MW;  7020A9AAF5CDBE8F CRC64;
     MSTTGNIAIT GIPTTAGPDG SFPLRRELRD LQRNYPDHFN LLVLALKDFQ ALNESVQTSY
     YQIAGIHGLP YKPWNNVGSN SDWQSTSGFG GYCTHSSILF LTWHRPYLAL FEQALYNSIQ
     KIANQFPQGP LRTKYVEAAK TFRMPYFDWA SQPPSGSSAF PSAFTAPSLQ VVDVDGKTKS
     TANPIYRFVF HPVNPSPGDF PRQWSRFPTT VRYPNPRTGQ SQDNRVAPIL ANELASLRTN
     VSLLLLSYTN FDAFSFNRWD PNMTPGEFGS LEDVHNEIHD RTGGGGHMSS LDVSSFDPLF
     WFHHTNVDRL WAIWQDLNPD NFLTPRPAPY STFNSTEGES QTKDTPLTPF WDKSATKFWT
     SEEIKDTTTT FGYAYPETQE WKYRTGSEYQ TSIRQAVTTL YGTNVFANFA AANVQARATE
     HTELIKSLSL AAPPPSAPIT AEKPLLITQE MKASPIPEHL QHLAPNNKYP EWVVNIRAQK
     HGLHGAFRVI VFLGPIDESD PDSWQTEFNT VGRVSVLGRS TQGPTTTKCA KCITDAADEL
     MISGTVPLTS ALLQDIVNEN TASIACSQRK WCRI