A0A397HQ89 · ANKC_ASPTH
- ProteinFAD-dependent monooxygenase ankC
- GeneankC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids587 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide (PubMed:36702957).
AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism (PubMed:36702957).
Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A (PubMed:36702957).
AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism (PubMed:36702957).
Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A (PubMed:36702957).
Catalytic activity
- AH2 + cyclo(L-arginyl-L-dehydrotyrosyl) + O2 = A + cyclo(L-arginyl-(Z)-dehydro-3,4-dihydroxytyrosyl) + H2OThis reaction proceeds in the forward direction.
Cofactor
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
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 ankC
- 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 accessionA0A397HQ89
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 7-27 | Helical | ||||
Sequence: AVDVLIIGAGPAGLIAAMWMA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460656 | 1-587 | FAD-dependent monooxygenase ankC | |||
Sequence: MTKKESAVDVLIIGAGPAGLIAAMWMAKCGITTRVVEQRPYQLRVGGADGIHPRSMEMFESFGIDQEITQVWEPITGWALWCRNAEGTLARSDRMDNPTPVRCRWGPGLLQQGIIERIIKEHISEQPSVRIEHETVSASLVIMEDALDKPDSHPCVITLRHDDSAGGSEELVRAKYVIGADGARSWTRKQLGFKMEGTRTRSVWAVTDLVVVSDFPDIRLCTTINSYGEGGLFFLRRERGLTRFYVQLNRADEVEFPAASITQELIIERLQRLLRPYTLTVKRCEWWSSYTVAHYLSDGMTKHDRVFLVGDAVHNHSPLVGLGMNISMQDSYNLGWKLAGVLKKELNPSILSTYETERRPVAAELIETDRFHLQLFDTATVTGSEPAWMLEREEALQPSMQGFAVHYQDPLLTVATEKECRPDAVIPGKRFPQLNVSNHATGKVYSIQSLLKSKGKFHVIVFAGDLSQPLELNRFNTCGTALQQIEEQILPASMGKFNVIAVHRARKTAIELASLADIFFPVDETTGRDYNRVYCDMETSYEEAGIGEQGAVVLVRPDQYVGWCGEVEDVQGLTGYLQPIFEAKKHA |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)65,803
- Last updated2018-12-05 v1
- Checksum0678F7F0C95B0FE6
Keywords
- Technical term