| IED ID | IndEnz0007000410 |
| Enzyme Type ID | catalase000410 |
| Protein Name |
Tryptophan dimethylallyltransferase EC 2.5.1.34 4-dimethylallyltryptophan synthase DMATS All-trans-hexaprenyl-diphosphate synthase L-tryptophan dimethylallyl transferase |
| Gene Name | dmaW TRV_01863 |
| Organism | Trichophyton verrucosum (strain HKI 0517) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton verrucosum (Cattle ringworm fungus) Trichophyton verrucosum (strain HKI 0517) |
| Enzyme Sequence | MGSIEIPNCSGSIVYKTISDFIDFPDHEQKLWWHSTAPMFAEMLRVAGYDLHSQYKILGIFLNHVIPFLGVYPTRINNRWLSILTRYGTPFELSLNCSQSLVRYTYEPINSATGTVKDPFNTHSIWDALDRLMPLQKGIDLEFFKHLKQDLTVDDQDSAYLLENNLVGGQIRTQNKLALDLKGGNFVLKTYIYPALKALATGKSIKTLMFDSVYRLCRQNPSLEAPLRALEEYVDSKGPNSTASPRLLSCDLIDPSKSRVKIYILELNVTLEAMEDLWTMGGRLNDASTLAGLEMLRELWDLIKLPPGMREYPEPFLQLGTIPDEQLPLMANYTLHHDQAMPEPQVYFTTFGLNDGRVADGLVTFFERRGWNHMA |
| Enzyme Length | 375 |
| Uniprot Accession Number | D4D449 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 92; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 103; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 189; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 191; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 193; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 246; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 259; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 261; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 263; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 345; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 347; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912, ChEBI:CHEBI:58209; EC=2.5.1.34; Evidence={ECO:0000250|UniProtKB:Q50EL0}; |
| DNA Binding | |
| EC Number | 2.5.1.34 |
| Enzyme Function | FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (PubMed:22403186). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186). {ECO:0000269|PubMed:22403186}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000305|PubMed:22403186}. |
| nucleotide Binding | |
| Features | Binding site (11); Chain (1); Region (1) |
| Keywords | Alkaloid metabolism;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,705 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14173 |
| Cross Reference Brenda |