ID A0A5N6ZG89_9EURO Unreviewed; 637 AA.
AC A0A5N6ZG89;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BDV28DRAFT_165407 {ECO:0000313|EMBL:KAE8356243.1};
OS Aspergillus coremiiformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=138285 {ECO:0000313|EMBL:KAE8356243.1, ECO:0000313|Proteomes:UP000327118};
RN [1] {ECO:0000313|Proteomes:UP000327118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 553.77 {ECO:0000313|Proteomes:UP000327118};
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 studyof 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 -!- 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}.
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DR EMBL; ML739041; KAE8356243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6ZG89; -.
DR Proteomes; UP000327118; 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:SF76; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
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:UP000327118}.
FT DOMAIN 95..112
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 397..408
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 637 AA; 72282 MW; 1F8C5810CC1E5DB6 CRC64;
MTIIVGGIKT RDAENKLCLR QDIDKWYVEQ DGGNRIQLTL FVEALALIQK RPLDNLLSYF
RLAAIHSAPL CEWDDVPQPR KTEGREDRIP GYCVHNDYTF PTWHRVYMML YERALYDAMG
EWIGTSVPAN LQATWKEEAD KWRLPYWDFA RFADRSLSTL GCASESGIEH DSCRLPILCM
MPNVRITVFH KDEDPTIESR PNPLYKYVTP KLMGELPPPY TITGEKVPEK RDEVSGKVTS
PGFTLPWDKC NASTKYGILD GFHASIWADG GQNWHRANYA LNEHPYYEDK DKGVNAGRPV
PTLQDLVYRL FQYGLSSWGA FSSTCFKSGI PEKEKPEGIE KYCPELDGDI KNALSLEFIH
NNVHNFVGGS QFPRPPKDGI HLWGTGHMSS VPVAAFDPIF FIYHCNIDRL TAMWQILNWD
KWFDDKESQK TLDKDLTPFH KDADRNFWKS DDKILEDIAT LYGNPTKTLF DRLPAAHGVQ
YDFVITVIYD KYALNGAPYK INLFLGATNN FRGPDSEGFV ASVYNFSGSL ESGACGNCQQ
QKKEGVMAIA QVPATVPVRY YLAKAGIDIP SSKNLPELVY MALNSLGNPV QMNEGDIHVE
LHTSQRAYYA HPFKPDDNDP LVYGFIKDGR QATGVFN
//
