A0A1L9WQQ1 · ACRE_ASPA1
- ProteinFAD-binding monooxygenase acrE
- GeneacrE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids593 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
FAD-binding monooxygenase; part of the cluster that mediates the biosynthesis of acurin A, a highly reduced polyketide coupled to a serine via a peptide bond (PubMed:32234543).
The activities of the highly reducing polyketide synthase acrA and the nonribosomal peptide synthetase acrB are collectively responsible for the synthesis of the acurin A core structure with a heptaketide backbone produced by acrA covalently fused to a L-serine by acrB (PubMed:32234543).
After the formation of the PK-NRP hybrid product, it is detached from acrB by reductive release to set up the formation of the lactam ring by aldol condensation (Probable). The hydrolyase acrC then catalyzes water loss to generate a double bond in the ring (Probable). This double bond is probably reduced, which is followed by three oxidations at C-22 to generate the carboxylic acid moiety, involving probably the FAD-binding monooxygenase acrE and the cytochrome P450 monooxygenases acrD and acrF (Probable). Finally, a last methylation step performed by the O-methyltransferase acrG leads to the production of acurin A (Probable)
The activities of the highly reducing polyketide synthase acrA and the nonribosomal peptide synthetase acrB are collectively responsible for the synthesis of the acurin A core structure with a heptaketide backbone produced by acrA covalently fused to a L-serine by acrB (PubMed:32234543).
After the formation of the PK-NRP hybrid product, it is detached from acrB by reductive release to set up the formation of the lactam ring by aldol condensation (Probable). The hydrolyase acrC then catalyzes water loss to generate a double bond in the ring (Probable). This double bond is probably reduced, which is followed by three oxidations at C-22 to generate the carboxylic acid moiety, involving probably the FAD-binding monooxygenase acrE and the cytochrome P450 monooxygenases acrD and acrF (Probable). Finally, a last methylation step performed by the O-methyltransferase acrG leads to the production of acurin A (Probable)
Cofactor
Note: Binds 1 FAD per subunit.
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 61-64 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TWRF | ||||||
Binding site | 71-73 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RVD | ||||||
Binding site | 73-74 | FAD (UniProtKB | ChEBI) | ||||
Sequence: DS | ||||||
Binding site | 79 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 200-206 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TGASGVQ | ||||||
Binding site | 223-224 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Site | 346 | Transition state stabilizer | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | N,N-dimethylaniline monooxygenase activity | |
Molecular Function | NADP binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-binding monooxygenase acrE
- 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 accessionA0A1L9WQQ1
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Abolishes the production of acurin A.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450425 | 1-593 | FAD-binding monooxygenase acrE | |||
Sequence: MHRELKEFSHPHGSTGIYEDNLQVDVLIVGAGFSGIYMLHELRKQGLKTVVYEAGSDLGGTWRFNCYPGARVDSQVPLYQFSIPETYKDWTWSTNYPDYKELRAYFDHVDKVLDIKKDVAFGSVVVDAQFDTSQSRWVVKTQDGRTAYAKYFIAAAGVSSKRYIPEWEGIENFKGPIHHTSFWPEHEVDVRGKRAAIIGTGASGVQVTQAWGPQAGHLKVFLRSPNYSIPMRRKELTADEQNQLKPIYPQLFDLREKTFTGALVDFSERSALEDSEAEREAFYEQRYQTGGFDFSTANYKDTMLNPVANRYLYDFWAKKTRARLNDERVKDLLAPVEPPYFFGGKRSSLETDFYEQFNRDTVELVDAKSNPIVGFTENGIKMQDGTVHEVDVVCLATGFDTTTGSMINLGVRSIHGTTLQEDWSQAAETYLGLTVSGYPNLFHLYGTHAPTLFSQAVTTIEVQGRWIVDAIKQMERQAIRSINPSREAAHAWKLQIRAFQNASFFPTVHSTYMGGSIPGKPFELVSYPAGMPMYARQIRDALPTFPGFEVVKADGEKVENLAPGGLEATTNFFERLFGMPPSSAKEDLAKQDH |
Expression
Induction
Expression is positively regulated by the acurin A cluster-specific transcription regulator acrR.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length593
- Mass (Da)66,932
- Last updated2017-03-15 v1
- ChecksumE660C64861D292B4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KV878980 EMBL· GenBank· DDBJ | OJJ98492.1 EMBL· GenBank· DDBJ | Genomic DNA |