Detail Information for IndEnz0007000278
IED ID IndEnz0007000278
Enzyme Type ID catalase000278
Protein Name Chanoclavine-I dehydrogenase easD
ChaDH
EC 1.1.1.332
Ergot alkaloid synthesis protein D
Oxidoreductase 2
Gene Name easD cpox2 CPUR_04080
Organism Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Claviceps Claviceps purpurea (Ergot fungus) (Sphacelia segetum) Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum)
Enzyme Sequence MPSMTSKVFAITGGASGIGAATCRLLAERGAAVICLADVSSTNFTSLQESIAKSNPSTLVHCTELDVRSADKVDQWLQSIVSTHGDLHGAANVAGIAQGAGLRATPTILEENDAEWSRILDVNLNGVFYSTRAQVRVMKDLPPGHRSIVNVASIAAFSHVPDVYAYGTSKSACAYLTTCIAADVFWSGIRVNCVSPGITNTPMLPQFEPKAKSLDEIKDMYRDQGYPTGEADGVARTIVWLLSEDSIPVYGANINVGACPP
Enzyme Length 261
Uniprot Accession Number M1VVW5
Absorption
Active Site ACT_SITE 166; /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:Q4WZ66};
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:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). 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:20118373, PubMed:21409592). 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 (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). 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:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048). {ECO:0000250|UniProtKB:Q50EL0, ECO:0000269|PubMed:10071219, ECO:0000269|PubMed:14700635, ECO:0000269|PubMed:14732265, ECO:0000269|PubMed:15904941, ECO:0000269|PubMed:16538694, ECO:0000269|PubMed:17560817, ECO:0000269|PubMed:19139103, ECO:0000269|PubMed:20118373, ECO:0000269|PubMed:20735127, ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:21494745, ECO:0000269|PubMed:24361048, ECO:0000305|PubMed:17308187, ECO:0000305|PubMed:17720822}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000305|PubMed:15904941}.
nucleotide Binding NP_BIND 16..40; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q12634
Features Active site (1); Chain (1); Glycosylation (1); Nucleotide binding (1); Signal peptide (1)
Keywords Alkaloid metabolism;Glycoprotein;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 27,619
Kinetics
Metal Binding
Rhea ID RHEA:33891
Cross Reference Brenda