ID G1XS72_ARTOA Unreviewed; 708 AA.
AC G1XS72;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-OCT-2025, entry version 56.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=AOL_s00210g230 {ECO:0000313|EMBL:EGX44069.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX44069.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX44069.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-dopa + O2 = 2 L-dopaquinone + 2 H2O; 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:ARBA00048233};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = L-dopaquinone + H2O; 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:ARBA00048881};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX44069.1}.
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DR EMBL; ADOT01000308; EGX44069.1; -; Genomic_DNA.
DR RefSeq; XP_011127334.1; XM_011129032.1.
DR AlphaFoldDB; G1XS72; -.
DR STRING; 756982.G1XS72; -.
DR GeneID; 22898236; -.
DR eggNOG; ENOG502R1BY; Eukaryota.
DR HOGENOM; CLU_013691_3_0_1; -.
DR InParanoid; G1XS72; -.
DR OMA; WQTIYPN; -.
DR OrthoDB; 6132182at2759; -.
DR Proteomes; UP000008784; 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 GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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; IPR050316; Tyrosinase/Hemocyanin.
DR InterPro; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF76; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR Pfam; PF18132; Tyrosinase_C; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..708
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003428022"
FT DOMAIN 206..223
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT REGION 69..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..94
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 78814 MW; 69DD464EC1B80ABD CRC64;
MAGWSSLKYA FIASSIFTIT SALPTDGLAR RDYQLQNEYN DYYAHDNNDY YNQGYRANSN
EPTSVKYQNK ATVAPRPSAT SSTPSTRTRT SNPRPNAPGP KADEGEYDPT SLEGFRGSYG
SDPKGPIIVT GVQNGQTAVR KEIRDLIKDH TQFSLFIMAL YRLQKQPQDM ETSYYGIAGI
HGAPFKSWGG VELKEGGNPE WGYCPHSDVL FLPWHRPYMA LIEQIMWKHA SDIVDGIPEG
PKKEKFKAVL PSLRFPYWDW AADGSIPEEV CQQNIIPIET VRNDRESIPN PLYAYNFSDL
SEFTNYPWGN VTETIRFPAK FGTPATHTRQ INEVMKASEG TWRNRVYQVL TGYKTFTSMA
STGYDRANGF RFESFEAIHG SVHLAVGQNL DGLGSGAILG VDGAMLGHMN PPVYSAFDPI
SWLHHINVDR VFNIWQTMNP NAYKFSGRTR MGTWAVPFNA AVDERTPLYP FKKSANEFFT
GADVENPKQF GYSYPETNSG NARDTLVAVN KLYGSRTPAF EIKNARDGSR RQKRQETNPV
ASVVDNSNKY TDWIINIEVN NGAEVGTFGI NAFLGEPSTD NAAKWITDPN SVGAHGVLTR
FDAHPDVLVT GTIPLTAALL KKVESKEIES LLPDVVIPYL LKNLKIKVRT ATDTIVEDLK
EVKDLKIEIV AGEVGLPKDM ATAPSYGDYQ TKIDWVDVAG GKLTPKPQ
//
