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Database: UniProt
Entry: K5UXV0_PHACS
LinkDB: K5UXV0_PHACS
Original site: K5UXV0_PHACS 
ID   K5UXV0_PHACS            Unreviewed;       602 AA.
AC   K5UXV0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=PHACADRAFT_259085 {ECO:0000313|EMBL:EKM54921.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54921.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM54921.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54921.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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:0000256|ARBA:ARBA00000426};
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:0000256|ARBA:ARBA00001038};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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DR   EMBL; JH930473; EKM54921.1; -; Genomic_DNA.
DR   RefSeq; XP_007397593.1; XM_007397531.1.
DR   AlphaFoldDB; K5UXV0; -.
DR   STRING; 650164.K5UXV0; -.
DR   GeneID; 18917302; -.
DR   KEGG; pco:PHACADRAFT_259085; -.
DR   HOGENOM; CLU_013691_3_0_1; -.
DR   InParanoid; K5UXV0; -.
DR   OrthoDB; 2785948at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.310.20; -; 1.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR016216; Monophenol_mOase_fun.
DR   InterPro; IPR041640; Tyrosinase_C.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF18132; Tyosinase_C; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PIRSF; PIRSF000340; MPO_fungal; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT   DOMAIN          90..107
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          283..294
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   602 AA;  64760 MW;  27FE3326AB7348D4 CRC64;
     MSHFVITGVQ GGSTADAGPP NRLEINDFVK IEDQFSLYIQ ALTAMSQDTQ GDLTSFFQIG
     AIHGLPYIQW DGSGGKEPVK NSQWGGYCTH GSVLFPTWHR PYVALFEQVL QQHAATIAKT
     YTVDQDRWNK AAADLRAPYW DWAVNSVPPP EVIADKQVTI TLPDGTRGAV NNPLYGYVFH
     PIDPSFPAPY NQWQSTLRHP ASDGPDAQTD VQALTDQLQS SQDDITSSTY RLLTRVHTWP
     AFSNHSTDDG GSASNSLEAI HDGIHVDVGG DGQMADPSVA GFDPIFFLHH ANVDRMLSLW
     SALNPGVWTT NGPAEGGTYT ITSNATVGPT TQLTPFWESQ SGYWLSSQTT ATGKLGYTYP
     EFNGLNVSDP RAVKAAIAKA VNSLYGGPSF GAFAAAAPGI AAFAAPAAIH ATPAVSKLAA
     PRNPQPSAES APNSVSDAAS SLYDWAVRIH VKKYELSGSF SVLIFLGPVP EDPREWRRSP
     SFVGAHHAFV NSSASQCANC HNQAAAGYVT EGFVHLNTAI ARLSEIHSFE PSVVEPYLKR
     ELSWRVVRAN KTAVDLNDVP SLEVVVCATQ LTLQPGADLP EHGTPQYFTG ITAGRQGGAR
     TE
//
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