ID A0A166AA12_9AGAM Unreviewed; 789 AA.
AC A0A166AA12;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=SISSUDRAFT_1064722 {ECO:0000313|EMBL:KZT35124.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT35124.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT35124.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT35124.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV428151; KZT35124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166AA12; -.
DR STRING; 1314776.A0A166AA12; -.
DR Proteomes; UP000076798; 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 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:UP000076798}.
FT DOMAIN 234..251
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 477..488
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 104..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 87011 MW; B098B5CDAE0FABEC CRC64;
MSDKSSNPLI KIDGTQVQVI SPTEQIFPDL FYFKGAIPHG LSPDDIAVHV TLDHSEEPIT
CEATLDCDKL VVTLTHKIVL TGPTKRRVAR SSGKGAWCLP SEIPGNGYPG SGQDTKEEGY
PTIPIPVPEP KPDDEEGGPD SKNSTYAIIG IRQGWGPAPE QVPLRYEVDE WYGNPANKDQ
INLFFLAMSR FQSLPPDAKL SYWQVCGIHS QPLVPWDEKT QSKTAGRGLG YCTHNSNLFP
LWHRSYMLLF EQRLFEIMRD DVIPEFPQNQ QAALLTAANQ WRFPYWDWAA KKARAGSNTP
VYDVPTIVTL PNIEVLTPTG LRTISNPVYA FKTAIAMGDP SLGANGLLQS TPPVCTLNYS
GKQMSTASRS SQKTLAYQAW VNGVQNNQEL ANNLRGLQLS QGGRFTDTLG ESVYRLFSEK
YFSSFSAFAL AFASTAHRQS QTPTDFSSLE SIHNNIHNSV GGTNGGHMSS PAVAAFDPNF
WFHHCNVDRQ FAIWQALNSD SWFEDPREQL ADPEGNWSTP PGAIPSPENT PLAPFHIDAV
GTYWTSNDAR EWLKYGYSYP ELQQWLPKYR TGGRFNQELY KADIAKQVNA LYSDTRQILL
TRGLQSSRGS RGSAGHILSS VEGVDRFALA GLSFTIHIYI GQDTCVGTLY NFSTPAHTTG
VNDGCENCRR QESGHALCTG QVPITSSLLK YVADDGVPLS SMEPEQVEAY LKKNLTWTVT
KAYGEDVPIS SISSLEVSLA VGTGCHYGGH SRLSKYHSYR VLPGCTEGRP GGYRRPNPPP
PRHAEAAFA
//
