ID A0A074YPA7_AURSE Unreviewed; 782 AA.
AC A0A074YPA7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=AUEXF2481DRAFT_61752 {ECO:0000313|EMBL:KEQ99530.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ99530.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ99530.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ99530.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584750; KEQ99530.1; -; Genomic_DNA.
DR RefSeq; XP_013348277.1; XM_013492823.1.
DR AlphaFoldDB; A0A074YPA7; -.
DR STRING; 1043005.A0A074YPA7; -.
DR GeneID; 25369522; -.
DR HOGENOM; CLU_013691_3_0_1; -.
DR InParanoid; A0A074YPA7; -.
DR OMA; NGYCTHV; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000030641; 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:SF132; 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:UP000030641};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..782
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001703404"
FT DOMAIN 133..150
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"
FT REGION 449..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 84172 MW; A33E941D3306C25B CRC64;
MRFQGVIGAA LLGSSALQHV AASTQPDVEG DLVNIDGYLV NAERLETRQS APAKIAVTGV
TGNGVQPRME LRTMQQQYPD MFNVFLLGLR SFMQMSQSDP LSYYQIAGIH GRPYVPWDGI
GSAPGFGGGY CTHTSNMFLP WHRPYLALIE QELYKHVQQA AQSFPAGATR NKYVAAAQNW
RYPYWDWAAA PCSSCKAFPA LLSDQWATVT TPTGIQTIAN PLFRYDFHPV SVSDMVYNPF
ASWDVTKRYP SSWDASAGSQ NNLLNPIFTN SQVNFRDRLY NLFTNYNNFH QFGDSAWITA
SSTNADSLES LHDGIHSSVG NNGHMTYLDY AAFDPVFWLH HVMVDRSFAL WQSIHTDSYV
QPLAAVGSTF TYPAGTINDV NSPLTPFFKD TAGTNWTSAD VRDTTKLGYT YPELQNGATA
ASVRAAINRL YGKNAVAADV SANVNLGNAA SSAPASSSTP AAPSAPAVPS ASAKPSGPTP
PVAPSRQNAQ RPGLASIWRS HPVHIWSPWW KRDNMTGEPY YNANGTNGTD EYHHEYICNI
VSQKFAMNGS YAVYVFLGNV SSNSTEELQL SPNLVGTYSV FSNMPSEDND MANMDLKITG
TVPLTTSLLG KYETGELRTM LPADVEPYLR KNLQWRVAKY DGGEVAVADV PDLSLNVVQA
QVTPAADETE FPQWGAFTAL TSVTAGKVGG YSAQYWNCPE DGSSFDNGYS GTPAAPQTPE
TPATSASAPY GNGTAASPVA PQGTAAGTGS VIPLSPTTYT GAANIVSMSG CAIALAAAAL
LI
//
