| IED ID | IndEnz0010001822 |
| Enzyme Type ID | esterase001822 |
| Protein Name |
Trichothecene 3-O-acetyltransferase TRI101 EC 2.3.1.- Trichothecene biosynthesis protein 101 |
| Gene Name | TRI101 |
| Organism | Fusarium sporotrichioides |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Fusarium sporotrichioides |
| Enzyme Sequence | MAATSSTSSQSFDIELDIIGQQPPLLSIYTQISLVYPVSDPSQYPTIVSTLEEGLKRLSQTFPWVAGQVKTEGISEGNTGTSKIIPYEETPRLVVKDLRDDSSAPTIEGLRKAGFPLEMFDENVVAPRKTLAIGPGNGPNDPKPVLLLQLNFIKGGLILTVNGQHGAMDMTGQDAIIRLLSKACRNESFTEEEISAMNLDRKTVVPLLENYKVGPELDHQIAKPAPAGDAPPAPAKATWAFFSFTPKALSELKDAATKTLDASSKFVSTDDALSAFIWQSTSRVRLARLDASTPTEFCRAVDMRGPMGVSSTYPGLLQNMTYHDSTVAEIANEPLGATASRLRSELNSDRLRRRTQALATYMHGLPDKSSVSLTADANPSSSIMLSSWAKVGCWEYDFGFGLGKPESVRRPRFEPFESLMYFMPKKPDGEFTASISLRDEDMERLKADEEWTKYAKYIG |
| Enzyme Length | 459 |
| Uniprot Accession Number | O94197 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 253; /note="Coenzyme A"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; BINDING 302; /note="Coenzyme A; via amide nitrogen"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; BINDING 318; /note="Coenzyme A"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; BINDING 343; /note="Coenzyme A"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; BINDING 386; /note="Coenzyme A"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; BINDING 390; /note="Coenzyme A"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: 3-O-acetyltransferase involved in the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:17923480). The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:10583973, PubMed:3800398). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333). TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519). Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042). During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042). More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533). Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973). TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973). A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041). A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated bythe acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533). A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047). Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755). {ECO:0000269|PubMed:10583973, ECO:0000269|PubMed:11352533, ECO:0000269|PubMed:12039755, ECO:0000269|PubMed:12135578, ECO:0000269|PubMed:12620849, ECO:0000269|PubMed:14532047, ECO:0000269|PubMed:16917519, ECO:0000269|PubMed:2317042, ECO:0000269|PubMed:3800398, ECO:0000269|PubMed:7651333, ECO:0000269|PubMed:8593041, ECO:0000269|PubMed:9435078}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis. {ECO:0000269|PubMed:10583973}. |
| nucleotide Binding | |
| Features | Beta strand (14); Binding site (6); Chain (1); Helix (20); Metal binding (4); Region (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Metal-binding;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2ZBA; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,336 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17.1 uM for isotrichodermol {ECO:0000269|PubMed:17923480}; KM=15.8 uM for T2-toxin {ECO:0000269|PubMed:17923480}; KM=1463 uM for deoxynivalenol (DON) {ECO:0000269|PubMed:17923480}; KM=350 uM for nivalenol (NIV) {ECO:0000269|PubMed:17923480}; |
| Metal Binding | METAL 218; /note="Calcium"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; METAL 221; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; METAL 376; /note="Calcium"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA"; METAL 449; /note="Calcium"; /evidence="ECO:0000269|PubMed:17923480, ECO:0007744|PDB:2ZBA" |
| Rhea ID | |
| Cross Reference Brenda |