Detail Information for IndEnz0007000542
IED ID IndEnz0007000542
Enzyme Type ID catalase000542
Protein Name Probable inactive reductase easA
Ergot alkaloid synthesis protein A
Gene Name easA
Organism Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Epichloe Epichloe festucae Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
Enzyme Sequence MSTSNLFTPLQFGKCLLQHKLVLSPMTRFRADNEGVPLPYVKTYYCQRASLPGTLLLTEATAISRRARGFPNVPGIWSQEQIAGWKEVVDAVHAKGSYIWLQLWATGRAAEVGVLKANGFDLVSSSAVPVSPGEPTPRALSDDEINSYIGDFVQAAKNAVLEAGFDGVELHGANGFLIDQFLQSPCNQRTDQWGGCIENRSRFGLEITRRVIDAVGKDHVGMKLSTWSTFQGMGTMDDLIPQFEHFIMRLREIGIAYLHLANSRWVEEEDPTIRTHPDIHNETFVRMWGKEKPVLLAGGYGPESAKLVVDETYSDHKNIGVVFGRHYISNPDLPFRLKMGLPLQKYNRETFYIPFSDEGYLDYPYSEEYITENKKQAVLA
Enzyme Length 380
Uniprot Accession Number A2TBU0
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 ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). 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). The presence of easA is not required to complete this reaction (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 (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979). {ECO:0000250|UniProtKB:Q50EL0, ECO:0000269|PubMed:11592979, ECO:0000269|PubMed:17308187}.
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 Alkaloid metabolism;FMN;Flavoprotein;NADP
Interact With
Induction INDUCTION: Strongly expressed in planta but not expressed in axenic culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 42,697
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda