| IED ID | IndEnz0016000040 |
| Enzyme Type ID | tyrosinase000040 |
| Protein Name |
N-acetyl-6-hydroxytryptophan oxidase ivoB AHTase ivoB EC 1.14.-.- Ivory mutation-related protein B Monophenol oxidase |
| Gene Name | ivoB ANIA_00231 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MHLLSSLAALAAAITVAFADVQQCNAENASVRKEWGSLTPDEQLGYIDAVWCLRSLPSRLPNEQYPGVQDRVDDFVATHINLTMVIHRNAPFLPWHRQYIHLWETALREECGYNGTVPYWNWTKNPDLYTNPVFDTTQSPETSLSLSGDGAYVAPSPTDPDPDPGLDFAPGRGGGCVLDGPFKDWPVRMGPFSAAQAYPYAPVPENAFAHNPRCLQRNLDVARIQYYNNPSVLESLLAAPSIAVFQDILDRTIPGTWQQAIGAHGGGHISVGPTLADVFASPQDPVFMLHHGFIDLLWDAWQRSGSDTGEGTDRMRALNGTTMYTNPPGAEEATLDTVMEFGVLGSPKKIGEVMDIRGGEYCYRYE |
| Enzyme Length | 366 |
| Uniprot Accession Number | Q5BGU9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by 2,3-dihydroxynaphthalene, phenylhydrazine, diethyl dithiocarbamate and 8-hydroxyquinolene (PubMed:2126551). {ECO:0000269|PubMed:2126551}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.14.-.- |
| Enzyme Function | FUNCTION: Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment (PubMed:23617571, PubMed:28108400). The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion (PubMed:31573806). While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function (PubMed:31573806). D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC (PubMed:28108400). N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.4). {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:23617571, ECO:0000269|PubMed:28108400, ECO:0000269|PubMed:31573806, ECO:0000269|Ref.4, ECO:0000305|PubMed:31573806}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:2126551}; |
| Pathway | PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:28108400, ECO:0000269|Ref.4}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (5); Metal binding (3); Signal peptide (1) |
| Keywords | Copper;Direct protein sequencing;Glycoprotein;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:2126551 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,299 |
| Kinetics | |
| Metal Binding | METAL 87; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 96; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 291; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | |
| Cross Reference Brenda |