A0A0U5CJT8 · AUSR_ASPCI

  • Protein
    Cytochrome P450 monooxygenase ausR
  • Gene
    ausR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725).
The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494).
3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494).
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 modifies austinolide to austinol (By similarity).
Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494).
The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494).
The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494).
The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-hydroxydehydroaustin (PubMed:28233494).
AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494).
Finally, the iron/alpha-ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494).

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 site439Fe (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 Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      ausR
    • ORF names
      ASPCAL14360

Organism names

  • Taxonomic identifier
  • Strain
    • SF006504
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes

Accessions

  • Primary accession
    A0A0U5CJT8

Proteomes

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane15-35Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Eesults in loss of 7-hydroxydehydroaustin and accumulates a new product, 1,2-dihydro-dehydroaustin.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004538421-500Cytochrome 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
    500
  • Mass (Da)
    56,502
  • Last updated
    2016-03-16 v1
  • Checksum
    C092DE80EE55DC66
MLRLMHPFSAQPNEGVGLYILWTVAVLFVIFKLLAPAKCDLPTVNGRRRFEIGQYQARRRFALDGRGIILNGLRKARAFRVVSQKGPKIILGPEFADEVKSHPACNADVFIAKEFHAHVSGFEVLRPQQVMKDAIRLKLTRSIGVLMKPMSAETALILETQWGNSDCWHELDLKSTIASLVSRVSAVMFVGEELGRDQKWLSIVTNYSSDMFVADLDLCKWPEALRPIATYFLSSCGKLRRHIREAALMLDPILSERYSAPHNKHNFLDWFEEVAGGRKYNPVLAQLSLAAAAIDTTSDLIIQTLTDICRFRDSGKLQQDLREEMVRVLRADGWEKSAMYNLKLLDSVLKETQRVKPVVVFGMGRYVTEQMTLHDGTVIPQGETINVVNTRVWDSAVYPNPLEWDPYRFVRRRDSGDHAAHLVSPTPDHMGFGLGKHSCPGRFFAATKIKILLCHILLKYDVKISDEASSTVVSSGNFLFPDATLSFCVRRRQDNLTIWG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CDMC01000024
EMBL· GenBank· DDBJ
CEL11257.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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