B8NI20 · IMQC_ASPFN
- ProteinFAD-dependent monooxygenase imqC
- GeneimqC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids223 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
function
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination (PubMed:29182847).
ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors (PubMed:29182847).
N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline (PubMed:29182847).
Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation (PubMed:29182847).
The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH (PubMed:29182847).
Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins (PubMed:29182847).
ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors (PubMed:29182847).
N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline (PubMed:29182847).
Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation (PubMed:29182847).
The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH (PubMed:29182847).
Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins (PubMed:29182847).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-dependent monooxygenase imqC
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionB8NI20
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000444551 | 1-223 | FAD-dependent monooxygenase imqC | |||
Sequence: MIENLRKRSTIEVEWRKQPVHMDIDLDQVDNPEAYPITVSVETSKDGSDPGLLWQPMHAERDSIVKETIHAKYVLGCDGARSWIRQRLGVSFIGDLTDSTWGVMDIVPKTSFPDIRKVAVIHSSKGTVMSVPREDKLVRFYIQIDAVNPNAASGLARRDLKVEDLLDAARAIMFPYTMEAAECAWWSAYRVGQRVANEFARHDRIFLAGDSVREYCLEVIRCQ |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length223
- Mass (Da)25,367
- Last updated2009-03-03 v1
- ChecksumE5634B522C36BE5B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EQ963479 EMBL· GenBank· DDBJ | EED49604.1 EMBL· GenBank· DDBJ | Genomic DNA |