Q4WAX1 · FTMH_ASPFU

Function

function

12-alpha,13-alpha-dihydroxyfumitremorgin C 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:18683158, 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)

Caution

In contrast to other A.fumigatus strains, strain ATCC MYA-4609 does not produce indole alkaloids such as fumitremorgins and verruculogen. While the biosynthetic pathway is complete, a variation in the O-methyltransferase FtmD (AC Q4WAW6) abolishes production of the tryprostatin A intermediate (PubMed:23649274).

Catalytic activity

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site94substrate
Binding site105dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site192dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site194dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site268dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site353dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site355dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site419dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site423dimethylallyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionprenyltransferase activity
Biological Processfumitremorgin B biosynthetic process
Biological Processverruculogen biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase
  • EC number
  • Alternative names
    • Fumitremorgin biosynthesis protein H

Gene names

    • Name
      ftmPT2
    • Synonyms
      ftmH
    • ORF names
      AFUA_8G00250

Organism names

Accessions

  • Primary accession
    Q4WAX1

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004241161-42712-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    48,530
  • Last updated
    2005-07-05 v1
  • Checksum
    B92E40E931C5F487
MTIPTEISCPEEDAFQLLDKFSWFPSDDQRRWWEYTGPYLLKLLRDAKYPQKDQVPCLYLLQQLLVPYLGTFPVVGQAPLPWWSNVTTYGVPFELSWNLLHNIVRIGFEPLSHLAESGVDAFNKTAPEECVSRLACLDNTIDLARFRHFQHHLLVTPEEETWLLKEKAPLAKSGRGQQTLAVEFQNGGISAKAYFFPGMKSLATGLSPGKLILDSIERLALPGLKEPVHHLRSTLGLQDDGHPTDTAIAPFLLGVDLCTPERSRLKFYVTDQVVSWDRVADMWTLRGKRLEDPQCADGLALLRKLWDLLAIPEGYRSNIRPDFAFGTPPPEDYRPVMMANWTLSPKKKFPDPQIYLLTVGMNDAVVMDALVAFYEVLGWTDLASTYKDKVASYFPGPDFTKTNYIHSGVSFSYRHSKPYLSVYYSPF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHF01000014
EMBL· GenBank· DDBJ
EAL85141.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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