A0A4P8DJE5 · DMXL3_CRYX8

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the dimeric xanthones cryptosporioptides (PubMed:30996871).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase dmx-nrPKS (Probable). The atrochrysone carboxyl ACP thioesterase dmxR1 then breaks the thioester bond and releases the atrochrysone carboxylic acid from dmx-nrPKS (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase dmxR15, and oxidized by the anthrone oxygenase dmxR16 to yield emodin (Probable). Emodin is then reduced to emodin hydroquinone by the oxidoreductase dmxR7 (Probable). A-ring reduction by the short chain dehydrogenase dmxR18, dehydration by the scytalone dehydratase-like protein dmxR17 and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:30996871).
Baeyer-Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) dmxR6 then yields monodictylactone in equilibrium with monodictyphenone (PubMed:30996871).
In the case of the cryptosporioptides biosynthesis, monodictylactone is reduced at C-12 to an alcohol (by the short chain dehydrogenases dmxR12 or dmxR8) and hydroxylated at C-5 by dmxR9, yielding the electron-rich aromatic which could eliminate H2O to form the ortho-quinonemethide, followed by tautomerisation to paraquinone and complete the formal reduction to produce the 10-methylgroup (Probable). Conjugate addition of C-4a-OH to the resulting paraquinone by the monooxygenase dmxR10 then gives cyclohexadienone, which is then reduced at C-5 by the short chain dehydrogenase dmxR3 to give the dihydroxanthone (Probable). The 6,7-epoxide in the cryptosporioptides could be introduced by the cytochrome P450 monooxygenase dmxL3 (Probable). The highly reducing PKS dmxL2 manufactures butyrate, which is further carboxylated by dmxL1 to form ethylmalonate (PubMed:30996871).
It is not yet clear whether the carboxylation occurs while the butyrate is attached to the ACP of dmxL2, but this unusual fungal metabolite could then be esterified to O-5 by the O-acetyltransferase dmxR13 (PubMed:30996871).
Finally, dimerization performed by dmxR5 gives the observed dimers cryptosporioptides A, B and C as the final products of the pathway (PubMed:30996871).

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site459Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 monooxygenase dmxL3
  • EC number
  • Alternative names
    • Dimeric xanthone biosynthesis cluster protein L3

Gene names

    • Name
      dmxL3

Organism names

Accessions

  • Primary accession
    A0A4P8DJE5

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane1-21Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004534751-514Cytochrome P450 monooxygenase dmxL3

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    58,013
  • Last updated
    2019-07-31 v1
  • Checksum
    AC89C11F1C5D0848
MALYLQIVGIIGGLYLVSTAFKILSRYSRSWKAARQHGCKPVKRYPNREPFLGSDLSRILKEENKRGKGLEAYANLHRTYGDTFAFKALSPTQLSTCDPKNIQTIATTNFDHWGVEPMRGDTLAPFLGPGVLTHDGQIWKRARANIRPTFNRAEVADLENFELYVSSLLGLIPRDGRTVDLAPLFKKLFLDTATEFIFGRSVGSLVPDSPFNALEFMKAFDASAIGLALRIKAGALKPLLFCFDKTWEKSYTQVHNFVDNQVRKALQPHSDLEKTEKLGHDSEQREKFILLDQMTKETRDPLVLRDQVLNVFMPARGVSATAISNIIFELARHPDSWESLQREVQSINGQPLTFDLIRSLKVAKTIVYETLRIHPPAPMIKRVALRDTILPTGGGPDQLSPVFVPKGTIISVHIYSVQTDPKIWGDDAKEFKPQRWAEGKPLWESKWQYEPFFAGPRMCPGQQMVLTQVTYLLVRLAQEFKGLENRDEVNEYLALGELTVQSKNGAKVSLTPAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK182094
EMBL· GenBank· DDBJ
QCL09088.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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