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 |