ID A0A0B7G4H1_THACB Unreviewed; 700 AA.
AC A0A0B7G4H1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=RSOLAG1IB_10992 {ECO:0000313|EMBL:CEL64009.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL64009.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL64009.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL64009.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; LN679193; CEL64009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7G4H1; -.
DR STRING; 1108050.A0A0B7G4H1; -.
DR Proteomes; UP000059188; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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:UP000059188}.
FT DOMAIN 320..331
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 700 AA; 78217 MW; 8398CAEED58D7E8F CRC64;
MTAPLLVTGA SVPGGVYPRL EIRELAKEKP EQFTLFILGW ERIRDPKFKP KAGQFQEIAG
IHGMPYVPWC GDPDEAMQTQ VICDVAQGIA GEYASKAGST EQAAAWLKAA RELRFPYWDW
THPGTGTEGF PEILKNDTVT IRDPTGQDVT YPNILSHYQF NESVDGFNNR MEVSEFQNLP
DPDNPPKEMA YFREWKRTWR RPNSSPVNVQ ENYAALDADL KNKSKTQRGE WEKGSWAQLT
NDVANMFSFP VDLPPELYAN AWDEFSNTTF QSGRKDSKNH SVFHSPFVQH ATPIEQPHNR
VHLIVGGLGH MGDNDTAGFD PIFYLHHCNV DRLISFWEQI FPYYVPGTDG YLDVDGETRV
PFSQAGGTYI ETPSQTVDSE TPLMPFRKSD NTYWTLKDTH LLRLTKENND PRIVQNKYYT
YNPIAGVELA TDDKVLPVKD REIQRGILQR HFGYNPVKVV KKNPKISFSA FSVESPSSYD
TQEEVDLPAG ASELEDFRQF LVEVSLSPQY HNSSYTLNLT VGTDNNHLDI GAVSVLGRGQ
SAGCGNCQAK RAANARVRGV IQIPYEAIVG ILQARYTEPP SSEVEVTADD TSALSTEKLV
RDLRLSIGSY VDLPSGKLHS ELSKKVGMSE SGNKGNDAAP SIRLLSCRVH KIDVGDKGEP
SFGFHDWQNH GSVIGTWEKS ARFALGVDRD AGLKHSGTAY
//
