Detail Information for IndEnz0007000296
IED ID IndEnz0007000296
Enzyme Type ID catalase000296
Protein Name FAD-linked oxidoreductase easE
EC 1.-.-.-
Chanoclavine I synthase
Ergot alkaloid synthesis protein E
Oxidoreductase 1
Gene Name easE ccsA cpox1 CPUR_04079
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 MERRQSICPQGRLPFYSAVVRSTSDIQASVRFASRHNLRLVIKNTGHDSAGRSSAPHSFQIHTSLLQNISLHKNFIARGSTTGRGPAVTLGAGVMQWQAYVHGAKNGYTILGGECPTVGAIGGFLQGGGVSSIHSFTRGLAVDQVLEYQVVSAKGDLITANEDNNQDLFWALKGGGGGTFGVVTEATVRVFSDDPVTVTSTKIEAAAANVLFWKEGVHELLRLLQRFNNLHVAGQLVISAPTKDSLQAGLELHFANLTDETQAIQLLRSEARALETHGISASTSVRVQRKASSELRMKPDLYPPHYGILEASVLISAATFHANDGPALIASKLSGLTLKPNDILFTSNLGGRVSENTAIEIALHPAWREAAQLVTLVRVVEPSIEGKLSALNDLTARDVPILYSIDPAAKISYRNLGDPQEKEFQARYWGADNYARLAATKAAWDPSHLFMTSLGVGSEVWDAEGICRKRRGFRAKASSLIGM
Enzyme Length 483
Uniprot Accession Number M1W0X9
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 1.-.-.-
Enzyme Function FUNCTION: FAD-linked oxidoreductase; 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:0000269|PubMed:20118373}.
nucleotide Binding
Features Chain (1); Domain (1); Erroneous initiation (1)
Keywords Alkaloid metabolism;FAD;Flavoprotein;Oxidoreductase;Reference proteome
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 52,072
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda