A0A2P1DP98 · MACF_PENTR
- ProteinFAD-dependent monooxygenase macF
- GenemacF
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids519 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of macrophorins, isoprenoid epoxycyclohexenones containing cyclized drimane moieties (PubMed:28926261).
The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase macA (PubMed:28926261).
6-MSA is then converted to m-cresol by the decarboxylase macB (By similarity).
The cytochrome P450 monooxygenase macC then catalyzes the oxidation of m-cresol to toluquinol (By similarity).
Epoxidation of toluquinol is then performed by the short chain dehydrogenase macD, with the help of macE, and a further prenylation by macG leads to 7-deacetoxyyanuthone A (By similarity).
The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield 22-deacetylyanuthone A (By similarity).
O-Mevalon transferase macI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (By similarity).
The terpene cyclase macJ catalyzes the cyclization of 22-deacetylyanuthone A to macrophorin A (PubMed:28926261).
MacJ is also able to catalyze cyclization of yanuthone E and 7-deacetoxyyanuthone A to their corresponding macrophorins (PubMed:28926261).
The macJ products can be further modified by macH and macJ, as well as by the FAD-dependent monooxygenase macF, to produce additional macrophorins, including 4'-oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E (PubMed:28926261).
The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase macA (PubMed:28926261).
6-MSA is then converted to m-cresol by the decarboxylase macB (By similarity).
The cytochrome P450 monooxygenase macC then catalyzes the oxidation of m-cresol to toluquinol (By similarity).
Epoxidation of toluquinol is then performed by the short chain dehydrogenase macD, with the help of macE, and a further prenylation by macG leads to 7-deacetoxyyanuthone A (By similarity).
The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield 22-deacetylyanuthone A (By similarity).
O-Mevalon transferase macI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (By similarity).
The terpene cyclase macJ catalyzes the cyclization of 22-deacetylyanuthone A to macrophorin A (PubMed:28926261).
MacJ is also able to catalyze cyclization of yanuthone E and 7-deacetoxyyanuthone A to their corresponding macrophorins (PubMed:28926261).
The macJ products can be further modified by macH and macJ, as well as by the FAD-dependent monooxygenase macF, to produce additional macrophorins, including 4'-oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E (PubMed:28926261).
Miscellaneous
The macrophorins cluster contains a single gene insertion (encoding for the terpene cyclase macJ) compared with the yanuthone cluster that produces the linear compound yanuthone.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-dependent monooxygenase macF
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A2P1DP98
PTM/Processing
Features
Showing features for signal, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MTKMTSIIGILMGVLTTATA | ||||||
Chain | PRO_5015136411 | 21-519 | FAD-dependent monooxygenase macF | |||
Sequence: ASIPTGSSAAAAAALGSLGVSPPSGNVLIGNAGYTCSLLNRVLSKNETFTVTSPYYDVLIDEAWSENCRLNASCIVTPESAEEVSRLLQILSILETRFAIRSGGHNTNPGFSSIGSDGVLIALEKLDSISLSADRGTVTVGPGNKWESVYKYLQPYNLTALGGREAVVGVGGYILGETGGLSTFYNTHGLAIDSVTRFQVVLPNGTIVDATPTEHADLYKGLKGGLNNFGIVTEYDLTTNTGVDIYYEIKTYTTANTPAVLAAYATYLLDADINSNVEIQINPSYTLVFYGYLGHVSAPTDFDPFSDIPVASTMYPPTNGSLTELLLSIGSTGLTSEGVSYSGTFSFKVTGSTFLQDTYSTYLEAAASLPTGAVLSYVPQGVIPNLVTQGKSQNGGNLLGLDATPQVWANIFVQFPATLSQSEVAGSVDSLLANLISSAKSEDLFLPYIFVNDAGAKQKPLQSFGEKNIKYIDTVAKRYDPKRIMQRLQNQAYFVLEEL | ||||||
Modified residue | 125 | Pros-8alpha-FAD histidine | ||||
Sequence: H |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 88-262 | FAD-binding PCMH-type | ||||
Sequence: CRLNASCIVTPESAEEVSRLLQILSILETRFAIRSGGHNTNPGFSSIGSDGVLIALEKLDSISLSADRGTVTVGPGNKWESVYKYLQPYNLTALGGREAVVGVGGYILGETGGLSTFYNTHGLAIDSVTRFQVVLPNGTIVDATPTEHADLYKGLKGGLNNFGIVTEYDLTTNTG |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length519
- Mass (Da)55,144
- Last updated2018-05-23 v1
- Checksum3975E83101269FC5