| IED ID | IndEnz0007000538 |
| Enzyme Type ID | catalase000538 |
| Protein Name |
Probable inactive dehydrogenase easA Ergot alkaloid biosynthesis protein A |
| Gene Name | easA |
| Organism | Claviceps fusiformis (Ergot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Claviceps Claviceps fusiformis (Ergot fungus) |
| Enzyme Sequence | MSSSNLFKPIPLGRKVLQHKVVLSPMTRFRADNDGVPLSYVKSYYGQRASIRGTLLITEAVAICPRAKGFSNCPGIWHQDQIAAWKEVVDEVHSKGSVIWLQLWATGRASDADTLKESGFHLESSSDVPVAPGEPVPRPLSEDEIESYIRDYVTGAINAVQGAGFDGIEIHGANGFLVDQFLQASCNTRADQWGGSIENRSRFGLEITRRVVDAVGKDRVGVKLSPWSTFQGMGTMDDLVAQFEHFISRLREMDIAYIHLVNTRWLEEEEPGIKTHPDVDNQTFVRMWGNKTPILLAGGYDADSARRLVDETYSDQNNIMVVFGRHYISNPDLPFRLRLGIPLQKYNRDTFYIPFSDEGYLDYPFCQEFLDQQDVDQVVVAA |
| Enzyme Length | 382 |
| Uniprot Accession Number | A8C7R3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 60; /note=FMN; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 102; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 171; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 171; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 174; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 223; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 299; /note=FMN; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 325; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 352; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Probable inactive dehydrogenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). 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 (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not encode a functional enzyme indicating that C.fusiformis terminates its ergot alkaloid pathway at elymoclavine (PubMed:17720822). {ECO:0000250|UniProtKB:Q6ZXC1, ECO:0000269|PubMed:17720822}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 25..27; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; NP_BIND 324..325; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70 |
| Features | Binding site (9); Chain (1); Nucleotide binding (2) |
| Keywords | FMN;Flavoprotein |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,938 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |