Detail Information for IndEnz0016000015
IED ID IndEnz0016000015
Enzyme Type ID tyrosinase000015
Protein Name Tyrosinase P
EC 1.14.18.-
Melanin biosynthesis protein B
Gene Name tyrP melB ATEG_03564
Organism Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus terreus Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Enzyme Sequence MGFYRNLVLVAASCTQALGLCPAPRCDSPDIRHEWGELSREDRLSYISAVQCMKDRPPELSVEEVPAVRSRYDDFTAVHINYTLQIHNSGIFLPWHRHFIWLWEKALREECGFTGTLPYWDWVMWPNLAASPLFDGTETSLSGDGEFNATEQPTELNPEPGLTITIPRGAGGGCVRTGPFKDWVINMGPFAFNESYEPALPDHAFDYNPRCLVRSLNDWVIQTYNNQTVVDTLLDSPDIVEFQNIMGGFPNPPIPIGPHAMGHRSLGPDMLDFFASPQDPAFWQHHGMVDRLWTVWQDADEPWRRFALNGSSTTWYKDDTPEVTLQTTVEFGILDEPRPLYELMSPTAGPYCYTYT
Enzyme Length 356
Uniprot Accession Number Q0CRX0
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Activity is inhibited by the presence of dithiothreitol (DTT). {ECO:0000269|PubMed:27133313}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 1.14.18.-
Enzyme Function FUNCTION: Tyrosinase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:28791090, PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313). The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313). {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:28791090, ECO:0000269|PubMed:29270299}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-7. {ECO:0000269|PubMed:27133313};
Pathway PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:28791090}.
nucleotide Binding
Features Chain (1); Erroneous gene model prediction (1); Glycosylation (5); Metal binding (5); Signal peptide (1)
Keywords Copper;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Metal-binding;Oxidoreductase;Reference proteome;Signal
Interact With
Induction INDUCTION: Expression is induced during conidiation. {ECO:0000269|PubMed:27133313}.
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Golgi apparatus lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Note=The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active. {ECO:0000269|PubMed:29270299}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:27133313}.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 40,470
Kinetics
Metal Binding METAL 87; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 96; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 203; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 263; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 286; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19
Rhea ID
Cross Reference Brenda