W6Q0S4 · IFGH_PENRF
- ProteinFumigaclavine B O-acetyltransferase ifgI
- GeneifgI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids484 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Fumigaclavine B O-acetyltransferase; 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
- fumigaclavine B + acetyl-CoA = fumigaclavine A + CoA
Pathway
Alkaloid biosynthesis; ergot alkaloid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acyltransferase activity | |
Biological Process | indole alkaloid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFumigaclavine B O-acetyltransferase ifgI
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionW6Q0S4
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000444547 | 1-484 | Fumigaclavine B O-acetyltransferase ifgI | ||
Interaction
Structure
Sequence
- Sequence statusComplete
- Length484
- Mass (Da)53,739
- Last updated2014-04-16 v1
- Checksum0AFC7D093301C8B3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG792016 EMBL· GenBank· DDBJ | CDM30153.1 EMBL· GenBank· DDBJ | Genomic DNA |