A0A1L9WUI4 · ANEE_ASPA1
- ProteinThiohydrolase aneE
- GeneaneE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids318 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Thiohydrolase; part of the gene cluster that mediates the biosynthesis of aculenes, a unique type of norsesquiterpenes that contain a nordaucane skeleton linked to an L-proline moiety and are of mixed biosynthetic origin (PubMed:31618514).
The pathway begins with the synthesis of dauca-4,7-diene by the terpene cyclase aneC using farnesyl pyrophosphate (FPP) as substrate (PubMed:31618514).
The cytochrome P450 monooxygenase aneF then performs the initial oxidation at C-12 of dauca-4,7-diene to yield asperaculane D (PubMed:31618514).
Asperaculane D is substrate of the cytochrome P450 monooxygenase aneD for C-10 hydroxylation to yield asperaculane E (PubMed:31618514).
The cytochrome P450 monooxygenase aneG then converts asperaculane E into aculene D via C-2 oxidation (PubMed:31618514).
The monomodular nonribosomal peptide synthtase aneB adenylates L-proline and the thiohydrolase aneE transfers this activated L-proline derivative to aculenes D and C to produce respectively aculenes B and A (PubMed:31618514).
The dioxygenase aneA converts aculene D into aculene C, and aculene B into aculene A by introducing the 5,6-alkene moiety (PubMed:31618514).
Asperculanes A, B, C and F, as well as 14-prolyl asperculane C, might be shunt products of the pathway (PubMed:31618514).
The pathway begins with the synthesis of dauca-4,7-diene by the terpene cyclase aneC using farnesyl pyrophosphate (FPP) as substrate (PubMed:31618514).
The cytochrome P450 monooxygenase aneF then performs the initial oxidation at C-12 of dauca-4,7-diene to yield asperaculane D (PubMed:31618514).
Asperaculane D is substrate of the cytochrome P450 monooxygenase aneD for C-10 hydroxylation to yield asperaculane E (PubMed:31618514).
The cytochrome P450 monooxygenase aneG then converts asperaculane E into aculene D via C-2 oxidation (PubMed:31618514).
The monomodular nonribosomal peptide synthtase aneB adenylates L-proline and the thiohydrolase aneE transfers this activated L-proline derivative to aculenes D and C to produce respectively aculenes B and A (PubMed:31618514).
The dioxygenase aneA converts aculene D into aculene C, and aculene B into aculene A by introducing the 5,6-alkene moiety (PubMed:31618514).
Asperculanes A, B, C and F, as well as 14-prolyl asperculane C, might be shunt products of the pathway (PubMed:31618514).
Catalytic activity
- aculene D + L-prolyl-[peptidyl-carrier protein] = aculene B + holo-[peptidyl-carrier protein]This reaction proceeds in the forward direction.
- aculene C + L-prolyl-[peptidyl-carrier protein] = aculene A + holo-[peptidyl-carrier protein]This reaction proceeds in the forward direction.
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameThiohydrolase aneE
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A1L9WUI4
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Abolishes the production of aculenes A and B and accumulates aculenes C and D.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000449096 | 1-318 | Thiohydrolase aneE | |||
Sequence: MTKDNEEKTYSEVEFLTVDGLKLRGRLYLGEANGPALVMAHGFNAVKEIVIPWAAEVFQKNGISVLLFDPRNYGESEGMPRQEVDPEKQIEDYFDAVTFLRQQPGIDPEAIGLWGVSTSGATAIGAACFDKRVRLIISVCPLIEATFREEMVPDVMAQIIREREALVAARTAGQQSPQPTLVPMINQVGVSPMGFNAIHGKNFYEEMPWFKETAPNFRPHTTTLTYYKMLRWHPLSNIRCLSPTPIQMLIPGKDDVCPTQEQLDFFEALPGPKRMEYYEDRNHHGLLLGSAFEGVMEAQVRFVQDVLAGKFALKSGSQ |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)35,671
- Last updated2017-03-15 v1
- Checksum3F55884F7927A802
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KV878977 EMBL· GenBank· DDBJ | OJJ99916.1 EMBL· GenBank· DDBJ | Genomic DNA |