B9WZX4 · FTME_ASPFM

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)

Catalytic activity

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site443Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processverruculogen biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fumitremorgin C synthase
  • EC number
  • Alternative names
    • Cytochrome P450 monooxygenase ftmP450-2
    • Fumitremorgin biosynthesis protein E

Gene names

    • Name
      ftmP450-2
    • Synonyms
      ftmE

Organism names

  • Taxonomic identifier
  • Strain
    • BM939
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati

Accessions

  • Primary accession
    B9WZX4

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane4-24Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004241221-526Fumitremorgin C synthase

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    526
  • Mass (Da)
    58,983
  • Last updated
    2011-04-05 v1
  • Checksum
    A9D616753BDA4B46
MERLPLSPAVLFLIIVLPILYLWIRYTAPARPHGKHLSLPPGPPRLPKIGNLHQVPRQIPWKKYKEWSDTYGPIMSVQLADTIAVVFSSWDLIKNHIERRNTIYSSRPSVPFFLHATGGLNASILPYGPEWKLQRAIRSSVLKPSMTVKYRDVQHVETTQLLHELLSTNDFPVCLRRCIASVFLTVAYGERCVDHAGLEAIDRLEELNRAIALHAEALFSGAAGILTQLVLPKALVDRLPVRWKKDADMLHNRLTADLVARTRAALVRPGWNWVKEFSMKDGIGSGDGDGEQGSKVELKRLAYMVGSLYEASMAASQALRVIILAGLLHPDATRRMHDELDAVVGTGRLPDFHDAAQLPYTQAFIKEAMRWRSLTPMGSPRATSDEDECRGYHIPCGATVLVNVWAINHDEAIFLDPFAFQPERWIENPDLPQLMYGMGQRACPGRHMGQDSLFLATARLFWAFDMALPDGADPIDQERFLDSGTTLAAFLPDFEVRFTPRSEKYQEVIENSMAVLPDVLSISATP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB436628
EMBL· GenBank· DDBJ
BAH23999.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp