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Database: UniProt
Entry: F9G0F0_FUSOF
LinkDB: F9G0F0_FUSOF
Original site: F9G0F0_FUSOF 
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
//
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