ID F9G0F0_FUSOF Unreviewed; 600 AA.
AC F9G0F0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=FOXB_12132 {ECO:0000313|EMBL:EGU77348.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU77348.1};
RN [1] {ECO:0000313|EMBL:EGU77348.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU77348.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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}.
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:EGU77348.1}.
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DR EMBL; AFQF01003007; EGU77348.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G0F0; -.
DR STRING; 660025.F9G0F0; -.
DR PaxDb; 5507-FOXG_12078P0; -.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 355..366
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 600 AA; 67928 MW; 1DEB8B4A67DF16D2 CRC64;
MKPPTSTGDS PKVANWEDDI LPMIKAPYWI TVDPEGVGQT WIGEMQYWGK WDLSNYDDVK
KRAVGIYKHL RSQAMPVTRN PDHYWPEAAL EVFRNWVNHG FPKDSTAEPS QSPVIPDPVD
PPIAYRVRRD IMSLSPEELV AYQTKLDDVL RVRELGSKWQ ELGVLHAYWC LHYQEATFMW
HRAYLRYVEE LMDFPIPYWN GFAKEAACST SKFAGIPPMF LEETYQHPSG ETRQNPLRFA
KALNGKSKDG KSSTVTRNPI LTEGPDAKGW KEKIELFKIY HDQIAHALEQ KTYTTSESAQ
HFGVPWANIT DFTDDQPDKD YPFRFDFDGL FEQVHDNFHG WVGPDMADNT YTAFDPIFLS
YHANMDRLAG IFMDANPENQ FTSRFPLQPF INNGTDIDYD DPRRWRYTTI GDMAKDTRAL
GYMYGEPASP DFSTRKTAEE RGVRRAVSSG GKAIVLPAGL PGQDMTAATN SLKSTKKREL
IPYVVFTEVG CTTSSYRIDV FTAGAESTAP DVVGNPDFIG QVTRLGMGRG RDGSGPPNTN
RCRKPTATRV LCAGKFKDSL SKGDALKIIV TDLETGKEVD EEEYTQMSGF VPKLAWLPDY
//