A1DA64 · FTMF_NEOFI
- ProteinVerruculogen synthase
- GeneftmOx1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids291 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:23109474).
The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmPS/ftmA (By similarity).
Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (By similarity).
The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (By similarity).
The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (By similarity).
FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (By similarity).
Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (By similarity).
Finally, verruculogen is further converted to fumitremorgin A by the verruculogen prenyltransferase ftmPT3 (PubMed:23109474).
The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmPS/ftmA (By similarity).
Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (By similarity).
The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (By similarity).
The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (By similarity).
FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (By similarity).
Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (By similarity).
Finally, verruculogen is further converted to fumitremorgin A by the verruculogen prenyltransferase ftmPT3 (PubMed:23109474).
Catalytic activity
- fumitremorgin B + AH2 + 2-oxoglutarate + 2 O2 = verruculogen + succinate + A + CO2 + H2O
Cofactor
Pathway
Mycotoxin biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dioxygenase activity | |
Biological Process | alkaloid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVerruculogen synthase
- 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 accessionA1DA64
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000424135 | 1-291 | Verruculogen synthase | |||
Sequence: MTVDSKPQLQRLAADVDVDLMCRLLEEDGAFILKDLLPLDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNNILINPVIHAICEGYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHHQPLEAPPISLSVIFPLTEFTEENGATEVILGSHRWMEVGTPERDQAVLATMDPGDVLVVRQRVVHAGGGNRTTTGDPRRVVLAYFNSCQLTPFETYRTMPRETVESMTVLGQRMLGWRTMKPSDPNIVGINIIDDKRLENVLQLKATDLPA |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length291
- Mass (Da)32,740
- Last updated2007-01-23 v1
- ChecksumBCCA28B1BA1AFE72
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS027694 EMBL· GenBank· DDBJ | EAW19754.1 EMBL· GenBank· DDBJ | Genomic DNA |