| IED ID | IndEnz0002014226 |
| Enzyme Type ID | protease014226 |
| Protein Name |
Proline iminopeptidase aneH PIP EC 3.4.11.5 Aculenes biosynthesis cluster protein HA |
| Gene Name | aneH ASPACDRAFT_43554 |
| Organism | Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus aculeatus Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) |
| Enzyme Sequence | MAVEQNIAPAKLIDRFSHDGPGKCRTSEWRFEVPLNHSKPDEGTVRLFARSIHCVLGVDDPELPWMLYLQGGPGLGCKTPLEYAWLPSILEKGYRVLFLDERGTGQSSPITAKTLAQQGDHKKQADLLKRFRADNIVRDCEAVRKHLYQDAPADQSKWSVMAASFGGFCAISYVSMFPNSLVEVFIGGGPCPMVNEPGQVIPRLFAVAARRNEVYYKKYPEDVGRVKRIIKYLKENKVALSKGTLTPERFQQLGVMLGLHGGIDYIHGVVQRTDNDLDMFKFLTAPTLDLIENSGMAHNVIYSLLQEPMYCQGKAGGWCADKCRKADPRFSLNERNAQIWFTGEAIFSDMFESYDELKDLKPVAELLARSSDWGQLYNEAQLARNEVPVYVATAVEDMYVSYDLGCHTASKVKNLQQVVNNTWYHDAVETKASEVMPALFALKEDRID |
| Enzyme Length | 448 |
| Uniprot Accession Number | A0A1L9WUM2 |
| Absorption | |
| Active Site | ACT_SITE 164; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P52279; ACT_SITE 397; /evidence=ECO:0000250|UniProtKB:P52279; ACT_SITE 425; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P52279 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme 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). {ECO:0000269|PubMed:31618514}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:31618514}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52279}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,390 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |