G3KLH4 · ADAC_ASPNG
- ProteinFAD-dependent monooxygenase adaC
- GeneadaC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids414 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960).
The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960).
The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960).
Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960).
The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960).
The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960).
Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960).
Catalytic activity
- 3-(2,4-dioxopentyl)-3,6,8,9-tetrahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + NADPH + O2 + H+ = 3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + NADP+ + H2OThis reaction proceeds in the forward direction.
Cofactor
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 32 | FAD (UniProtKB | ChEBI) | |||
Binding site | 43 | FAD (UniProtKB | ChEBI) | |||
Binding site | 115 | FAD (UniProtKB | ChEBI) | |||
Binding site | 325 | FAD (UniProtKB | ChEBI) | |||
Binding site | 338 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | monooxygenase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-dependent monooxygenase adaC
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionG3KLH4
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000446347 | 1-414 | FAD-dependent monooxygenase adaC | ||
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length414
- Mass (Da)45,561
- Last updated2011-11-16 v1
- Checksum18980F105D1DC4E3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JN257714 EMBL· GenBank· DDBJ | AEN83887.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
OGUI01000016 EMBL· GenBank· DDBJ | SPB51662.1 EMBL· GenBank· DDBJ | Genomic DNA |