A0A0U5GGX2 · AUST_ASPCI
- ProteinShort chain dehydrogenase ausT
- GeneausT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids411 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Short chain dehydrogenase; 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).
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.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 105 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 137 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 249 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 249 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 253 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 263 | Proton donor | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | oxidoreductase activity | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameShort chain dehydrogenase ausT
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A0U5GGX2
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453871 | 1-411 | Short chain dehydrogenase ausT | |||
Sequence: MVDKSNKVALVLGATGISGWALAKNALSYPSRSTFQRVIGLMHRPRTVEETGLPNDPRLELYSGVDLQGDLNHVVVKLKEKIPRIEEVTHVYYLAYMTLQTCSGDMRQFRDANVAMTYTAVHACDRLCPNMEFFVLQTGTNAYGVACFDYLRQTQLQVPLRESNPRVPRPWSDTLFYYAQADLIKEANKGKAWKWCEVRPDQIVGHTPAQVSVPYVAPMALYLALYRYINGPGARVQFPGTVRNYHHTYTDVRPDTMARAELYLSLVKSDESHGEAFNIADTDTPGPWSAKWPSICRYFGLEASETIDDEWTDIDGWWYANQTAYERMCAEYGLQKQVMSPTAWSLMKMGHTLIDQNRELCLDKIRGLGFTEDHPVGSSYFQVFEDFERMKIIPPKVVLASPRCRDVLHQC |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)46,849
- Last updated2016-03-16 v1
- Checksum0FCED3863BE12CB4
Keywords
- Technical term