Q4WAZ0 · PSOF_ASPFU
- ProteinDual-functional monooxygenase/methyltransferase psoF
- GenepsoF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids905 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Dual-functional monooxygenase/methyltransferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566).
The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566).
The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566).
Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566).
The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566).
Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566).
The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566).
Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566).
The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566).
Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 18 | FAD (UniProtKB | ChEBI) | |||
Binding site | 45-48 | FAD (UniProtKB | ChEBI) | |||
Binding site | 55-57 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 57 | FAD (UniProtKB | ChEBI) | |||
Binding site | 63 | FAD (UniProtKB | ChEBI) | |||
Binding site | 110 | FAD (UniProtKB | ChEBI) | |||
Binding site | 185-191 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 208-209 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 328-329 | NADP+ (UniProtKB | ChEBI) | |||
Site | 329 | Transition state stabilizer | |||
Binding site | 495 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | methyltransferase activity | |
Molecular Function | monooxygenase activity | |
Molecular Function | N,N-dimethylaniline monooxygenase activity | |
Molecular Function | NADP binding | |
Biological Process | fumagillin biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual-functional monooxygenase/methyltransferase psoF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WAZ0
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000438200 | 1-905 | Dual-functional monooxygenase/methyltransferase psoF | ||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 12-215 | FAD-containing monooxygenase (FMO) domain | |||
Region | 695-876 | Methyltransferase (MT) domain | |||
Domain
PsoF is a unique bifunctional enzyme catalyzing two different types of reactions at completely separate steps of the pseurotin biosynthetic pathway and comprised an unusual combination of two domains, one homologous to a methyltransferase (MT) and another to an FAD-containing monooxygenase (FMO) (PubMed:24939566).
Sequence similarities
In the N-terminal section; belongs to the FAD-binding monooxygenase family.
In the C-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length905
- Mass (Da)101,032
- Last updated2005-07-05 v1
- ChecksumB3ACE4152EAE7487
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000014 EMBL· GenBank· DDBJ | EAL85122.1 EMBL· GenBank· DDBJ | Genomic DNA |