IED ID | IndEnz0007000555 |
Enzyme Type ID | catalase000555 |
Protein Name |
Chanoclavine-I dehydrogenase easD ChaDH EC 1.1.1.332 Ergot alkaloid synthesis protein D |
Gene Name | easD MCYG_06052 |
Organism | Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Microsporum Arthroderma otae (Microsporum canis) Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
Enzyme Sequence | MASVSSKIFAITGGASGIGAATCHLLARRGAAALCIGDLSNENMKQLEKSIREINPETKVHCTVLDVSSSSEVDKWVKDIISTFGDLHGAANVAGIAQGAGMRQIPTLLEEDDEQWKKVFQVNLDGILYATRAQVRAMKDSSSTSPGDRSIVNVASIASMAHMPDVFAYGTSKAGCAYFTTCVAQDVIPLGIRANTVSPGITRTPMLPRFVPNAKTQEEVEETYKKEGFSVIEADDVARTIVWLLSEDSRPVFGTNINVGACMP |
Enzyme Length | 264 |
Uniprot Accession Number | C5FTN0 |
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:0000250|UniProtKB:D4AK45}; |
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:0000305|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 | 28,214 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:33891 |
Cross Reference Brenda |