A0A1L9WUM2 · ANEH_ASPA1

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).

Catalytic activity

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site164Nucleophile
Active site397
Active site425Proton donor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaminopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Proline iminopeptidase aneH
  • EC number
  • Short names
    PIP
  • Alternative names
    • Aculenes biosynthesis cluster protein HA

Gene names

    • Name
      aneH
    • ORF names
      ASPACDRAFT_43554

Organism names

Accessions

  • Primary accession
    A0A1L9WUM2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004490971-448Proline iminopeptidase aneH

Interaction

Subunit

Homooligomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain64-191AB hydrolase-1

Sequence similarities

Belongs to the peptidase S33 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    448
  • Mass (Da)
    50,390
  • Last updated
    2017-03-15 v1
  • Checksum
    FD6A225B825371E7
MAVEQNIAPAKLIDRFSHDGPGKCRTSEWRFEVPLNHSKPDEGTVRLFARSIHCVLGVDDPELPWMLYLQGGPGLGCKTPLEYAWLPSILEKGYRVLFLDERGTGQSSPITAKTLAQQGDHKKQADLLKRFRADNIVRDCEAVRKHLYQDAPADQSKWSVMAASFGGFCAISYVSMFPNSLVEVFIGGGPCPMVNEPGQVIPRLFAVAARRNEVYYKKYPEDVGRVKRIIKYLKENKVALSKGTLTPERFQQLGVMLGLHGGIDYIHGVVQRTDNDLDMFKFLTAPTLDLIENSGMAHNVIYSLLQEPMYCQGKAGGWCADKCRKADPRFSLNERNAQIWFTGEAIFSDMFESYDELKDLKPVAELLARSSDWGQLYNEAQLARNEVPVYVATAVEDMYVSYDLGCHTASKVKNLQQVVNNTWYHDAVETKASEVMPALFALKEDRID

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV878977
EMBL· GenBank· DDBJ
OJJ99919.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp