B9WZX3 · FTMB_ASPFM

Function

function

Brevianamide F prenyltransferase; 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:16000710, 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: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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
55 μMbrevianamide F
74 μMdimethylallyl diphosphate

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site94brevianamide F (UniProtKB | ChEBI)
Binding site102brevianamide F (UniProtKB | ChEBI)
Binding site113dimethylallyl diphosphate (UniProtKB | ChEBI)
Site115Required for regioselectivity
Binding site201dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site203dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site205brevianamide F (UniProtKB | ChEBI)
Binding site294dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site296dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site380dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site382dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site446dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site450dimethylallyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionprenyltransferase activity
Biological Processverruculogen biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Tryprostatin B synthase
  • EC number
  • Alternative names
    • Brevianamide F prenyltransferase
    • Fumitremorgin biosynthesis protein B

Gene names

    • Name
      ftmPT1
    • Synonyms
      ftmB

Organism names

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

Accessions

  • Primary accession
    B9WZX3

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004241121-464Tryprostatin B synthase

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    52,607
  • Last updated
    2009-04-14 v1
  • Checksum
    75B775A0420B6D5B
MPPAPPDQKPCHQLQPAPYRALSESILFGSVDEERWWHSTAPILSRLLISSNYDVDVQYKYLSLYRHLVLPALGPYPQRDPETGIIATQWRSGMVLTGLPIEFSNNVARALIRIGVDPVTADSGTAQDPFNTTRPKVYLETAARLLPGVDLTRFYEFETELVITKAEEAVLQANPDLFRSPWKSQILTAMDLQKSGTVLVKAYFYPQPKSAVTGRSTEDLLVNAIRKVDREGRFETQLANLQRYIERRRRGLHVPGVTADKPPATAADKAFDACSFFPHFLSTDLVEPGKSRVKFYASERHVNLQMVEDIWTFGGLRRDPDALRGLELLRHFWADIQMREGYYTMPRGFCELGKSSAGFEAPMMFHFHLDGSQSPFPDPQMYVCVFGMNSRKLVEGLTTFYRRVGWEEMASHYQGNFLANYPDEDFEKAAHLCAYVSFAYKNGGAYVTLYNHSFNPVGDVSFPN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB436628
EMBL· GenBank· DDBJ
BAH23998.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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