A0A1L9WUM2 · ANEH_ASPA1
- ProteinProline iminopeptidase aneH
- GeneaneH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids448 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Proline iminopeptidase; 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
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 164 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 397 | |||||
Sequence: D | ||||||
Active site | 425 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aminopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProline iminopeptidase aneH
- EC number
- Short namesPIP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A1L9WUM2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000449097 | 1-448 | Proline iminopeptidase aneH | |||
Sequence: MAVEQNIAPAKLIDRFSHDGPGKCRTSEWRFEVPLNHSKPDEGTVRLFARSIHCVLGVDDPELPWMLYLQGGPGLGCKTPLEYAWLPSILEKGYRVLFLDERGTGQSSPITAKTLAQQGDHKKQADLLKRFRADNIVRDCEAVRKHLYQDAPADQSKWSVMAASFGGFCAISYVSMFPNSLVEVFIGGGPCPMVNEPGQVIPRLFAVAARRNEVYYKKYPEDVGRVKRIIKYLKENKVALSKGTLTPERFQQLGVMLGLHGGIDYIHGVVQRTDNDLDMFKFLTAPTLDLIENSGMAHNVIYSLLQEPMYCQGKAGGWCADKCRKADPRFSLNERNAQIWFTGEAIFSDMFESYDELKDLKPVAELLARSSDWGQLYNEAQLARNEVPVYVATAVEDMYVSYDLGCHTASKVKNLQQVVNNTWYHDAVETKASEVMPALFALKEDRID |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 64-191 | AB hydrolase-1 | ||||
Sequence: PWMLYLQGGPGLGCKTPLEYAWLPSILEKGYRVLFLDERGTGQSSPITAKTLAQQGDHKKQADLLKRFRADNIVRDCEAVRKHLYQDAPADQSKWSVMAASFGGFCAISYVSMFPNSLVEVFIGGGPC |
Sequence similarities
Belongs to the peptidase S33 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length448
- Mass (Da)50,390
- Last updated2017-03-15 v1
- ChecksumFD6A225B825371E7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KV878977 EMBL· GenBank· DDBJ | OJJ99919.1 EMBL· GenBank· DDBJ | Genomic DNA |