A0A0F7TN11 · AUSR_PENBI

  • Protein
    Cytochrome P450 monooxygenase ausR
  • Gene
    ausR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725).
The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity).
3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity).
Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity).
Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity).
Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity).
The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity).
The cytochrome P450 monooxygenase ausG then modifies austinolide to austinol (By similarity).
Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725).
The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725).
The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725).
Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725).

Miscellaneous

In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives.

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Secondary metabolite biosynthesis; terpenoid biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site435Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processmycotoxin biosynthetic process
Biological Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 monooxygenase ausR
  • EC number
  • Alternative names
    • Austinoid biosynthesis clusters protein R

Gene names

    • Name
      ausR
    • ORF names
      PMG11_06813

Organism names

  • Taxonomic identifier
  • Strain
    • MG11
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A0F7TN11

Proteomes

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-32Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004538431-496Cytochrome P450 monooxygenase ausR

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    56,255
  • Last updated
    2015-07-22 v1
  • Checksum
    D1A82BC730A48EAA
MHSFSTLPNHRIGLYILWTIPVLFVIFKLLAPAKCSLPIVNGRRWFEIGQYQARRRFSLDGRGIILKGLQKARAFRVVSQKGPKIILGPEYANEVKSHPACNADVFIAKEFHAHVSGFEVLRPQHVMKDAIRLKLTRSIGALMRPISDETTLILETQWGNSNCWHELDLKSTIAALVSRVSAVMFVGEELGRDQKWLSIVTNYSSDMFVADLDLCKWPEILRPIATYFLSSCGKLRRHIQEAALMLDPILSEGNSTHGNKQNFLDWFEEIAGGRKYNPVLAQISLAAAAIDTTSDLIIQTLTDICRFPDSEKLQEELREEMVRVLRADGWEKSAMYNLKLLDSVLKETQRVKPVVVFGMGRYVTEQITLHDGTVIPKGETINVVNTRVWDSAVYENPLEWDPYRFLRRRDSGDHAAHLVSPTPDHMGFGLGKHSCPGRFFAATKIKILLCHILLKYDVKISDEASSKVVSSGNFLFPDATLRISVRRRQENLSIWD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CDHK01000006
EMBL· GenBank· DDBJ
CEJ58143.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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