A0A1L9WLF1 · AACUM_ASPA1

Function

function

Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer secalonic acid D (PubMed:30996871, PubMed:33891392).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase AacuL (Probable). The atrochrysone carboxyl ACP thioesterase AacuM then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase AacuI, and oxidized by the anthrone oxygenase AacuG to yield emodin (Probable). Emodin is then reduced to emodin hydroquinone by a yet unidentified oxidoreductase (Probable). A-ring reduction by the short chain dehydrogenase AacuN, dehydration by the scytalone dehydratase-like protein AacuK and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:33891392).
Baeyer-Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) AacuH then yields monodictyphenone (PubMed:33891392).
Monodictyphenone is transformed into compounds with the tetrahydroxanthone skeleton via methylesterification by the methyltransferase AacuQ, followed by the action of the flavin-dependent monooxygenase AacuC, the isomerase AacuP, and the short chain dehydrogenase/reductase AacuF or AacuD (PubMed:33891392).
AacuF and AacuD should accept the same compound as a substrate but perform the ketoreduction with a different stereoselectivity, thus yielding blennolides B and A, respectively (PubMed:33891392).
In the final step of the biosynthesis, the cytochrome P450 monooxygenase AacuE accepts blennolide B and/or blennolide A to conduct the dimerization reaction to furnish the tetrahydroxanthone dimers, secalonic acids D, B, and F (PubMed:33891392).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Biotechnology

Secalonic acids show unprecedented anticancer activities against various human cancer cells and might be interesting for further derivatization, targeting diseases such as cancer.

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site103Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site105Zn2+ 1 (UniProtKB | ChEBI); catalytic
Active site107Proton donor/acceptor
Binding site107Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site108Zn2+ 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Biological Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Atrochrysone carboxyl ACP thioesterase AacuM
  • EC number
  • Short names
    ACTE AacuM
  • Alternative names
    • Secalonic acid biosynthesis cluster protein M

Gene names

    • Name
      AacuM
    • ORF names
      ASPACDRAFT_33688

Organism names

Accessions

  • Primary accession
    A0A1L9WLF1

Proteomes

Organism-specific databases

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004534311-312Atrochrysone carboxyl ACP thioesterase AacuM

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    312
  • Mass (Da)
    34,766
  • Last updated
    2017-03-15 v1
  • Checksum
    13A86B161887CD50
MGEGGYRQINKTLNVCAFDDYLVTQQSRLPKLLDIEQLSPRVLRVLGQNAGKFTLQGTNTYIVGTGQHRLIIDTAQGYREWADLIDVTLSNRSISLSHVFLTHWHGDHTGGVPDLIRMYPHLADGIYKNSPEQGQHPIEEGQIFKVEGATIRAVHGPGHSHDHMCFVLEEENAMFTGDNVLGHGTSAVEQLGLYMDTLRKLQAQGCRTGYPAHGAVIPDLNLKIATELAQKTRREKQCLAALGRIRKERPTGQLASVTVGELIDVVHGTRVNEEVRKMALEPFMEEVLRKLAEDGKVAFRVRKGVKTWFALT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV878984
EMBL· GenBank· DDBJ
OJJ96971.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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