B9WZX7 · FTMH_ASPFM

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)

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 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

Organism names

  • Taxonomic identifier
  • Strains
    • BM939
    • NIH 5233 / ATCC 13073
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati

Accessions

  • Primary accession
    B9WZX7
  • Secondary accessions
    • D3TIT5

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004241141-42712-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    48,584
  • Last updated
    2009-04-14 v1
  • Checksum
    26F23D63CE60F100
MTIPTEISCPEEDAFQLLDKFSWFPSDDQRRWWEYTGPYLLKLLRDAKYPQKDQVPCLYLLQQLLVPYLGTFPVVGQAPLPWWSNVTTYGVPFELSWNLLHNIVRIGFEPLSHLAESGVDAFNKTAPEECVSRLACLDNTIDLARFRHFQHHLLVTPEEETWLLREKAPLPKSGRGQQTLAVEFQNGGISAKAYFFPGMKSLATGLSPGKLILDSIERLALPGLKEPVHHLRSTLGLQDDGHPTDTAIAPFLLGVDLCTPERSRLKFYVTDQVVSWDRVADMWTLRGKRLEDPQCADGLALLRKLWDLLAIPEGYRSNIRPDFAFGTPPPEDYRPVMMANWTLSPKKKFPDPQIYLLTVGMNDAVVMDALVAFYEVLGWTDLASTYKDKVASYFPGPDFTKTNYIHSGVSFSYRHSKPYLSVYYSPF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict165in Ref. 2; ACF22981
Sequence conflict171in Ref. 2; ACF22981

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB436628
EMBL· GenBank· DDBJ
BAH24002.1
EMBL· GenBank· DDBJ
Genomic DNA
EU622826
EMBL· GenBank· DDBJ
ACF22981.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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