ID A0A1Y2VHR9_9PEZI Unreviewed; 615 AA.
AC A0A1Y2VHR9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=M434DRAFT_388779 {ECO:0000313|EMBL:OTA96924.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA96924.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA96924.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA96924.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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};
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DR EMBL; KZ112429; OTA96924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VHR9; -.
DR STRING; 1001938.A0A1Y2VHR9; -.
DR Proteomes; UP000194361; 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; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF32; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..615
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012305411"
FT DOMAIN 129..146
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 334..345
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 615 AA; 68939 MW; 872D4BEE4727394C CRC64;
MSFARQVCFF ITSFFFFFTV VADFVQPGQY DYGFNVDLRL RKREPTQSHI VTGLPRVDGQ
TQLRPDIRDL QKDEDKWNLY LLTLNWLQYT NQDSPFSWYQ ITGIHGAPAL TWGDVGPTPG
NEHSGYCTHV SILFPTWHRP YLALYEQVLY NIAQFVASLY PPDLQDRFQK AASTFRIPYW
DWAATPPDGV SVLPLAVGGS SSVNVSGPNG VQSISNPLFS YVFRPFNAST FPDFPYNTWH
ETKRAPRPVN SPNATSNNSF VAHALDTHLP SFQQRLYNLF SNYPNYTTFS NEAWIPSGNN
NDSYDSIESL HDAIHTVGGG VYGHLAIIAY SGFDPLFWLH HANVDRIFTM WQALYNDTYV
VPQPAVYSSH TTSPGESEDS QTGLTPFFSN ETHFWTSDMA RDHEVFGYTY AEVANKSRAE
VAASINRLYG NFSPISMLTR PTTNGLSWNG MTSAYPPVEA VFSGDKYREW IANIRVSKHA
MGGSFSIHLF LEDVPSDPIS WPVASNLVGT MGVFAHKGVH GSKSHRMVAG TIPITSALMQ
MVASGKIPSL HAEDIEPYLR LNLELRVSLV NGTEVDAHEV SGLHIEIASS MVKAPESESM
LSEWGKVERH FDLFA
//