ID A0A0A1T3I6_9HYPO Unreviewed; 552 AA.
AC A0A0A1T3I6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=VHEMI07414 {ECO:0000313|EMBL:CEJ91721.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ91721.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ91721.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000004; CEJ91721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1T3I6; -.
DR STRING; 1531966.A0A0A1T3I6; -.
DR HOGENOM; CLU_013691_2_0_1; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000039046; 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:UP000039046};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..552
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001978835"
FT DOMAIN 292..303
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 552 AA; 61518 MW; 5D9229634A797C98 CRC64;
MLPKTVLISV FFALTSALDQ KVATIGAWPA SQDGAVPIRQ NINKLHADGG PQWDLYIQAL
RMMQDANEDD PFSYFQLAGI HGLPFIEWGN TGGRNNATGW GGYCPHGEAM FLPWHRPYIV
LYEQIVVNNA RAIAETYPEA QREIYRNAAD QLRVPFWDWG VDGKVPDAVV PEMITIKASR
DGTVKDVTIP NPLATFVYPK SYGAGKYGPP PIETERVLRC QAPYSFPATA NANLQRRNYR
QRVYDVFSRA ETFDSFGTVG NKGISLESLH NNIHWDAACD HALVAPSTSG FDPIFFLHHA
NVDRLWAYWG AMKGDEGSLI QPYVGGPRWS TPNGTTINPD TTLQPFFDQN NQWYTIKSVA
DVDAFGYTYE GLEFWRKSDE QMKEDATTII NTLYGPRTPK VRRGGSLIPR ASDNTRLFAE
ISVEASELKD RPCEIEITVK GYKANSIVVL AHPVSGPVYG GFSLDEDESA NTFSAQSVEE
TVSSLDDNMQ IAIIKPDGTR LDASQILSLQ VDIEEVDVTP RQKDTEMPVV SLPRVHEAVR
AGKKLPNKRR NL
//