| IED ID | IndEnz0007000279 |
| Enzyme Type ID | catalase000279 |
| Protein Name |
Cytochrome P450 monooxygenase easM EC 1.-.-.- Ergot alkaloid synthesis protein M |
| Gene Name | easM AFUA_2G18010 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MDFLQRILGILSSEDVAPALFASSISVLFLILSYQVLYPPSKYSAFPTINGTRWLALSNRRILAEFVTDAQGLMRNGLEKYDIFRIISSIGPMTILHPKYTDEIHNDRQLNFMAVLAKEMFPNYPGFDLFREGTDGSTVLQDAVKFGSSRCLGKSTQLLSDETSTLLQKLWGDEPEWHEVTAKSSVHDIIAHLSALLFYGPELCSHKEWLEVTDEYASVGFLAARQLRLWPPILRPIAQWFLPACRRLRYLASRTRGLIEPVIAARQKEKAICYSHGRQPPVYDDAIEWTERAAKGRPYDAAMSPLLFSINALHTTTDLLTQVILDLSTQPDLIVALRQEILSVKPQQNGWKNASLNQLLLMDSAIKESQRLKPTESILMRRYAMDDLTLADGNKIPKGTVLGIPIFGMRDPKIYVDPDMYDGYRFQKMRDKPGFENKCQLVSTSPWHLGFGHGIHACPGRFLAAVQVKIILCYIVAKYDFKLAGGAPPKVQSVGIELISDTEARLAVRRRQEMVIGLE |
| Enzyme Length | 519 |
| Uniprot Accession Number | Q4WZ65 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909). {ECO:0000250|UniProtKB:B6D5I7, ECO:0000269|PubMed:15870460, ECO:0000269|PubMed:15933009, ECO:0000269|PubMed:19672909, ECO:0000269|PubMed:20039019, ECO:0000269|PubMed:20526482, ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:26972831}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000269|PubMed:26972831}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (2); Metal binding (1); Transmembrane (1) |
| Keywords | Alkaloid metabolism;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996). {ECO:0000269|PubMed:19028996}. |
| 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 | 58,532 |
| Kinetics | |
| Metal Binding | METAL 458; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:P04798 |
| Rhea ID | |
| Cross Reference Brenda |