| IED ID | IndEnz0002007440 |
| Enzyme Type ID | protease007440 |
| Protein Name |
Aspartic protease-like protein pynH EC 3.4.23.- Pyranonigrin biosynthesis cluster protein H |
| Gene Name | pynH An11g00310 |
| Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| 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 niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| Enzyme Sequence | MFPCSRIWSLLVAAATASAVPTSLATTHLQSVDLLLTRSSYGFLTDIALGTPGQSLPYLVDWTWTGHYVVTTLCYNDPTATYDCLNVDQKIFNQTLSSTFINQTDQYGYLYWDPNHFYFTEPAAADVATDMLRIGPTAVNTTIQAANFVFNETISAFPFSGVYGLSPVFQGDNRSVQASFYQGWRSGAWHSPIVSFIYCHDNATKAVCSGYDGLQTLGGYNTSHVQGDITWYDIIVTEAINTLDFVYAPAVINYWALNLTRFSIGDEEQELNKTTTLDGKQAAVAAFDHASYGRGAPVSVYGYQRLVELVGAKAVTLSDPPNNGEQGFYQFDCRNSSLLPPLRYEFAGSERAWEIVPENYVEVLANGTNKCTFNVRTLGDGAMVMGNFGETFAIDKYVMFDFEKLQVGIADFAW |
| Enzyme Length | 414 |
| Uniprot Accession Number | A5ABG6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic protease-like protein; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP (PubMed:24106156). The enoyl reducrase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine (PubMed:24106156, PubMed:26414728). Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J (PubMed:26414728). The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E (PubMed:26414728). {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728, ECO:0000305|PubMed:24106156}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26414728}. |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Glycosylation (11); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,782 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |