| IED ID | IndEnz0002013857 |
| Enzyme Type ID | protease013857 |
| Protein Name |
FAD-dependent monooxygenase pytG EC 1.-.-.- Pyranterreones biosynthesis cluster protein G |
| Gene Name | pytG ATEG_00918 |
| Organism | Aspergillus terreus (strain NIH 2624 / FGSC A1156) |
| 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 terreus Aspergillus terreus (strain NIH 2624 / FGSC A1156) |
| Enzyme Sequence | MSATTLPNVSVAIIGAGIGGLTLGAFLRRLGIPFVILERTAVLTPLGAGISLAPNCLAALEQLGLYETIRQNAQELRGINVYREKRCWGTIDFGLAKQWFGYNVLSIERYEFHRYLYEAAGGAGVVQLGWDVARIEGLENADGDLRVISADGREVHTDIVVGADGIRSVTRRILSRSMGLQPENTIRFTGRVHMSGYTKPLSHLSTTDLGIGHWMLYNDCILTTWPCKENRQWFIGVKAAPPDEKSPDRSVWKGATSDTVNAVYGSRFHPFGEDGTVEASMYAIPAPAIAGNSRDDKLSIIPNASSLATSSRKPTSRTWFGAEWRSWVMVYRT |
| Enzyme Length | 333 |
| Uniprot Accession Number | Q0CZG6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 19; /note=FAD; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:A6T923; BINDING 132; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A6T923 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo-methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). {ECO:0000269|PubMed:32077283, ECO:0000305|PubMed:32077283}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32077283}. |
| nucleotide Binding | NP_BIND 38..39; /note=FAD; /evidence=ECO:0000250|UniProtKB:A6T923; NP_BIND 294..298; /note=FAD; /evidence=ECO:0000250|UniProtKB:A6T923 |
| Features | Binding site (2); Chain (1); Glycosylation (1); Nucleotide binding (2); Region (1); Transmembrane (1) |
| Keywords | FAD;Flavoprotein;Glycoprotein;Membrane;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Expression is positively regulated by the cluster-specific transcription factor pytR. {ECO:0000269|PubMed:32077283}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,581 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |