| IED ID | IndEnz0007000446 |
| Enzyme Type ID | catalase000446 |
| Protein Name |
Chanoclavine-I dehydrogenase easD ChaDH EC 1.1.1.332 Ergot alkaloid synthesis protein D |
| Gene Name | easD ARB_04646 |
| Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Enzyme Sequence | MASVSSKIFAITGGASGIGAATCRLLAKRGAATLCVGDLCSENMKQLENDIKEINPNTKVHCTVLDVSSSSNVDEWIKDIITTFGDLHGAANIAGIAQGAGLRQAPTILEEDDQQWKKVFQVNLDGVLYSTRAQVRAMKESSSTNPGDRSIVNVASIASMSHMPDVFAYGTSKAGCAYFTTCVSQDVMPFGIRANTVSPEEVEETYKKEGFSVIEADDVARTIVWLLSEDSRPVFGANINVGACMP |
| Enzyme Length | 246 |
| Uniprot Accession Number | D4AK45 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q12634 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) + NADH; Xref=Rhea:RHEA:33891, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:71487, ChEBI:CHEBI:72949; EC=1.1.1.332; Evidence={ECO:0000269|PubMed:22403186}; |
| DNA Binding | |
| EC Number | 1.1.1.332 |
| Enzyme Function | FUNCTION: Chanoclavine-I dehydrogenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). 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 (PubMed:22403186). 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:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186). {ECO:0000269|PubMed:22403186}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000269|PubMed:22403186}. |
| nucleotide Binding | NP_BIND 16..40; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q12634 |
| Features | Active site (1); Chain (1); Nucleotide binding (1); Signal peptide (1) |
| Keywords | Alkaloid metabolism;NAD;Oxidoreductase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,236 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for chanoclavine-I {ECO:0000269|PubMed:22403186}; KM=0.36 mM for NAD(+) {ECO:0000269|PubMed:22403186}; |
| Metal Binding | |
| Rhea ID | RHEA:33891 |
| Cross Reference Brenda | 1.1.1.332; |