IED ID | IndEnz0007000425 |
Enzyme Type ID | catalase000425 |
Protein Name |
4-dimethylallyltryptophan N-methyltransferase easF EC 2.1.1.261 4-dimethylallyltryptophan methyltransferase Ergot alkaloid synthesis protein F |
Gene Name | easF TRV_01861 |
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 | MGSINPPQILDIRRSKFEESIPKQVEAGLLSSPKTLPALLFYSTEGIQHWNRYSHASDFYPRHEEIQILKDKATDMAASIADGSVVVDLGSASLDKVIHLLEALEAAQKKVTYYALDLSFSELTSTLQAIPTDQFVHVQFSALHGTFDDGLQWLKETLVIRDQPHCLLLFGLTIGNFSRPNAAKFLHNIASHALVESPSQSSILLTLDSCKVPTKVIRAYTAEGVVPFALESLKYGNTLFQQDAGENVFDPEDWYFLSEWNYVLGRHEASLVPRSKDIKLGRPLDKIVVGKHEKVRFGCSYKYDSEERKELFGTAGLRDVKSWSKEGCDVAFYQLKCCPN |
Enzyme Length | 340 |
Uniprot Accession Number | D4D447 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine = 4-(3-methylbut-2-enyl)-L-abrine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:34435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58209, ChEBI:CHEBI:59789, ChEBI:CHEBI:67248; EC=2.1.1.261; Evidence={ECO:0000250|UniProtKB:B6D5I7}; |
DNA Binding | |
EC Number | 2.1.1.261 |
Enzyme Function | FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; 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 | Chain (1); Erroneous initiation (1) |
Keywords | Alkaloid metabolism;Methyltransferase;S-adenosyl-L-methionine;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 | 38,117 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:34435 |
Cross Reference Brenda |