ID W7N554_GIBM7 Unreviewed; 669 AA.
AC W7N554;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=FVEG_10660 {ECO:0000313|EMBL:EWG51772.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG51772.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG51772.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022256; EWG51772.1; -; Genomic_DNA.
DR RefSeq; XP_018757963.1; XM_018899822.1.
DR AlphaFoldDB; W7N554; -.
DR STRING; 334819.W7N554; -.
DR EnsemblFungi; FVEG_10660T0; FVEG_10660T0; FVEG_10660.
DR GeneID; 30068233; -.
DR KEGG; fvr:FVEG_10660; -.
DR VEuPathDB; FungiDB:FVEG_10660; -.
DR eggNOG; ENOG502S1EE; Eukaryota.
DR HOGENOM; CLU_013691_3_0_1; -.
DR OMA; KYEWSRR; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000009096; Chromosome 11.
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 PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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:UP000009096}.
FT DOMAIN 346..357
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 669 AA; 76349 MW; CCD73BD394777851 CRC64;
MSSPNMDQLD KAHKEGVVLG LAGFGTAQRL DIDVMLTEQP DTFNLYLIAL MELQGMENLP
WPAPEGYSFK AGGDDLKMSW FQMTGIHGQP VSIWDGEGPR GYYCTHSRPH FGTWHRPYLA
MMEQTLFRQV ANVAKRFSES DIPDEQKKRY LDAARQFRLP YWDYYRPRAY TKTRFPGVIN
KDGTTTAPFD WGAPQIFTLP EVMVRRLPDN ELVPMANPFF QFEFSQDQLD KIKADRDPRR
RIKPQFENIL KTIRHGGSDE KATERMNKKL NKVREDELRI CLALMEDEVY RNYRTFSTNA
VLKPGEKPTA MLEEASGSIE DFHGGYHVTI GDPSGHMGSI ATAAFDPIFW MHHCQIDRLF
AIWQAANGDE HWFNELLLEE DQELATIDLT PFRKSVSENK EKTYWTSNLS RETKTFGYTY
PDTARGQTGD TIRKEFREKY EWSRRTTVKP VFGTPPDDMQ PIQVGDAQVF QYTSDTSSGD
LLKNPGVPFH EMQQQTVMAA MSSNTQYADD WYIDVVVERM LANGTYTIYY IIGDVQGQTG
EEWSTLPGFA GLSHILAAPT NVCDNCANQG EQGQLVTSTT AITSLLLDYV QIGKLNSMGE
GDVKKFLIDN LKWRVQTISG EVLNPRDMDR DHTFNLSISR KRTPVPRSAG DVQYDTYPEV
IEAIIRNSS
//
