Q4WAZ0 · PSOF_ASPFU

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).

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site18FAD (UniProtKB | ChEBI)
Binding site45-48FAD (UniProtKB | ChEBI)
Binding site55-57NADP+ (UniProtKB | ChEBI)
Binding site57FAD (UniProtKB | ChEBI)
Binding site63FAD (UniProtKB | ChEBI)
Binding site110FAD (UniProtKB | ChEBI)
Binding site185-191NADP+ (UniProtKB | ChEBI)
Binding site208-209NADP+ (UniProtKB | ChEBI)
Binding site328-329NADP+ (UniProtKB | ChEBI)
Site329Transition state stabilizer
Binding site495NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionmethyltransferase activity
Molecular Functionmonooxygenase activity
Molecular FunctionN,N-dimethylaniline monooxygenase activity
Molecular FunctionNADP binding
Biological Processfumagillin biosynthetic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dual-functional monooxygenase/methyltransferase psoF
  • EC number
  • Alternative names
    • Pseurotin biosynthesis protein F

Gene names

    • Name
      psoF
    • ORF names
      AFUA_8G00440

Organism names

Accessions

  • Primary accession
    Q4WAZ0

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Abolishes the production of pseurotin but leads to the accumulation of demethyl-deepoxy-synerazol (PubMed:24082142, PubMed:24939566).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004382001-905Dual-functional monooxygenase/methyltransferase psoF

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region12-215FAD-containing monooxygenase (FMO) domain
Region695-876Methyltransferase (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 status
    Complete
  • Length
    905
  • Mass (Da)
    101,032
  • Last updated
    2005-07-05 v1
  • Checksum
    B3ACE4152EAE7487
MTRIRPDYDAIVIGAGFSGVRSLWELRRLGLTARCFDAGSDVGGTWWWNRYPGCRTDGEAWVYALKFLPELLEEWDFTERYPPQEEIQWYLSRVLDRYDLRKDIEFNTEVKSAHYSDHDSIWKITTASGKVATARYFLPATGITSIPKEPPFPGLQSFKGEVYQTSTWPAHEIEFENKRIGVIGTGSTGIQVITKLAPVAEQLIVFQRTPNYVIPAQNYPLDEKKREDIKKTFDATWDIAKRNLAGHAVKHSGRMVASAGGPEEIQRVFEDGWARGCYDFQLGTFDDSFMDPHANAVTSDFIRQKIRSIVRDGDTAEVLCPTYPFGARRPPCADGYYETFNRSNVKLVDIREDEIEVYDQGIKTASGAEYELDMIILALGFDTGTGAMNKIDIRGSQNRSLRESWTRRLETFAGVLVHGYPNMFVVCGPHLPAGNQPVSLEAFASWIGKTIEHMETNGLASIDVSNEAMDAWTTHVEQVWGGSFLAKHAHEQGSWFVGTNIPGKPSRIMFYFGGMVNLEPWLIKELETGWSSMSFTRLDGAEASNGVSKQTVGGVHVTPEMLESVQIPLEADKVGMTPAEKSKLVNAATAVYIDMAVEEMRSRGLAPKADYRVHWWKVMQDFVDSGEGQRVLQETSLTNQELERVIAKLGIEGEVIARMGPEIVNILTGKTHALAHIMRDDLLFRVYLSDEGRRANRYMAEYARLLTSQRRDIRILEIGAGTGGTTSEVLNLCSPNGESFCAEYMYTDLSPGFFNAAKTTLKKWESHLAFQVLNIEDDPAGQGFKEHTYDLIIAANVIHATARLTNTLSNVHKLLKPGGVFGLVELTRLTPFYNLTFGSLSGWWAGVDEGRTESPLQSPQQWNSLLKQTGFSGVDLAAYDLPGPERHSCLLLSTALSNSVTTNGH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHF01000014
EMBL· GenBank· DDBJ
EAL85122.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp