B9WZX4 · FTME_ASPFM
- ProteinFumitremorgin C synthase
- GeneftmP450-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids526 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Cytochrome P450 monooxygenase; 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:19226505, PubMed:23649274).
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 ftmA (PubMed:16755625).
Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579).
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 (PubMed:19226505).
The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158).
Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315).
In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable)
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 ftmA (PubMed:16755625).
Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579).
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 (PubMed:19226505).
The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158).
Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315).
In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable)
Catalytic activity
- tryprostatin A + reduced [NADPH--hemoprotein reductase] + O2 = fumitremorgin C + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
Cofactor
Pathway
Mycotoxin biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
Biological Process | verruculogen biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFumitremorgin C 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 accessionB9WZX4
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 4-24 | Helical | ||||
Sequence: LPLSPAVLFLIIVLPILYLWI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000424122 | 1-526 | Fumitremorgin C synthase | |||
Sequence: MERLPLSPAVLFLIIVLPILYLWIRYTAPARPHGKHLSLPPGPPRLPKIGNLHQVPRQIPWKKYKEWSDTYGPIMSVQLADTIAVVFSSWDLIKNHIERRNTIYSSRPSVPFFLHATGGLNASILPYGPEWKLQRAIRSSVLKPSMTVKYRDVQHVETTQLLHELLSTNDFPVCLRRCIASVFLTVAYGERCVDHAGLEAIDRLEELNRAIALHAEALFSGAAGILTQLVLPKALVDRLPVRWKKDADMLHNRLTADLVARTRAALVRPGWNWVKEFSMKDGIGSGDGDGEQGSKVELKRLAYMVGSLYEASMAASQALRVIILAGLLHPDATRRMHDELDAVVGTGRLPDFHDAAQLPYTQAFIKEAMRWRSLTPMGSPRATSDEDECRGYHIPCGATVLVNVWAINHDEAIFLDPFAFQPERWIENPDLPQLMYGMGQRACPGRHMGQDSLFLATARLFWAFDMALPDGADPIDQERFLDSGTTLAAFLPDFEVRFTPRSEKYQEVIENSMAVLPDVLSISATP |
Structure
Sequence
- Sequence statusComplete
- Length526
- Mass (Da)58,983
- Last updated2011-04-05 v1
- ChecksumA9D616753BDA4B46