W6QL00 · IFGB_PENRF
- Protein4-dimethylallyltryptophan N-methyltransferase ifgB
- GeneifgB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids340 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28620689).
The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:28620689).
The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689).
The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217).
The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:28620689, PubMed:28902217).
The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689).
Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689).
Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217).
The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217).
The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:28620689).
The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689).
The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217).
The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:28620689, PubMed:28902217).
The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689).
Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689).
Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217).
The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217).
Catalytic activity
- 4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine = 4-(3-methylbut-2-enyl)-L-abrine + S-adenosyl-L-homocysteine + H+
Pathway
Alkaloid biosynthesis; ergot alkaloid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | methyltransferase activity | |
Biological Process | indole alkaloid biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-dimethylallyltryptophan N-methyltransferase ifgB
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionW6QL00
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000444537 | 1-340 | 4-dimethylallyltryptophan N-methyltransferase ifgB | ||
Interaction
Structure
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)37,904
- Last updated2014-04-16 v1
- Checksum6C47190C75C1D5C0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG792019 EMBL· GenBank· DDBJ | CDM36676.1 EMBL· GenBank· DDBJ | Genomic DNA |