Detail Information for IndEnz0007000544
IED ID IndEnz0007000544
Enzyme Type ID catalase000544
Protein Name 4-dimethylallyltryptophan N-methyltransferase easF
EC 2.1.1.261
4-dimethylallyltryptophan methyltransferase
Ergot alkaloid synthesis protein F
Gene Name easF ARB_04647
Organism Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes)
Enzyme Sequence MGSINPPQILDIRRSKFEESIPKQVEAGLLSSPKTLPALLFYSTEGIQHWNRHSHASDFYPRHEEIQILKDKATDMAASIADGSVVVDLGSASLDKVIHLLEALEAAQKKVTYYALDLSFSELTSTLQAIPTDQFVHVQFSALHGTFDDGLQWLKETPVIRDQPHCLLLFGLTIGNFSRSNAAKFLHNIASHALVESPSQSSILLTLDSCKVPTKVTRAYTAEGVVPFALESLKYGNTLFQQDGGENVFDPEDWYFLSEWNYVLGRHEASLVPRSKDIKLGRPLDKIVVGKHEKVRFGCSYKYDSEERKELFGTAGLRDVKSWSKEGCDVAFYQLKCCPN
Enzyme Length 340
Uniprot Accession Number D4AK46
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)
Keywords Alkaloid metabolism;Methyltransferase;Reference proteome;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 38,039
Kinetics
Metal Binding
Rhea ID RHEA:34435
Cross Reference Brenda