ID A0A5N6U8N1_9EURO Unreviewed; 557 AA.
AC A0A5N6U8N1;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BDV25DRAFT_135307 {ECO:0000313|EMBL:KAE8154968.1};
OS Aspergillus avenaceus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=36643 {ECO:0000313|EMBL:KAE8154968.1, ECO:0000313|Proteomes:UP000325780};
RN [1] {ECO:0000313|EMBL:KAE8154968.1, ECO:0000313|Proteomes:UP000325780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 18842 {ECO:0000313|EMBL:KAE8154968.1,
RC ECO:0000313|Proteomes:UP000325780};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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; ML742025; KAE8154968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6U8N1; -.
DR Proteomes; UP000325780; 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; PS00497; TYROSINASE_1; 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:UP000325780}.
FT DOMAIN 63..81
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 309..320
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 557 AA; 63412 MW; 9F91C1CA29BDD3A9 CRC64;
MPTRKNIRDL STEELDKLIK AFKGIQDKHP EDPDSFFHIA GYHGQPFRGA GYENSDWWGG
YCHHGNVLFP TWHRAYLWRL EKALQTVPGC GDVTIPFWNQ VKDDEIPPIF LKRRYEFQNK
DKIDNPLYSY KLQRGFYDKL ARTVKAEQEN GADQAPEEQL VDYGKFFHYE TVRYPYSGLV
GPQDIRTTEL HNEVISQLGD ETVNGLLNLR ICQWLQGTNR TPGIRTQYNQ CLRAPNYTVF
SNTTSATKYN DDHSPHSSGL AECEEPLVCP IEKPHNGMHL AVGGYDMADN RDYSGANGDM
GENDTASFDP IFFFHHCFID LVFWSWQVSK GKTEKLEITP FYPGTNSVDS QGPTPGMLAG
EWLSMKTPLH PFMKYEDNNT QLPFTSEDVV DISRLGYSYD KSDILQPHKE DERQTLITST
LRVSGIDRGL IAGSFVILVC EKASQDLKSE EQKPKVVGYE PVFSRWHVAG CANCRNSLSV
TFHAPIAKVT SATTGEKLLD PIPDTSKVDY EVRLLTNDRK TGKKTIWAPD PQPPMDLVER
KFEVPLPKTR LRSVVVR
//
