Detail Information for IndEnz0007000277
IED ID IndEnz0007000277
Enzyme Type ID catalase000277
Protein Name Catalase easC
EC 1.11.-.-
Ergot alkaloid synthesis protein C
Gene Name easC
Organism Claviceps fusiformis (Ergot fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Claviceps Claviceps fusiformis (Ergot fungus)
Enzyme Sequence MASQVSLTAQGSGLSAPLNGPEHLTSTTVENDPRLLDILSRFNREKIPERAVHARGAGAYGEFEVTHDVSDICDIDMLLGIGKKTPCAVRFSTTALERGSAESVRDVKGMAIKLFTGDGEWDWVCLNIPMFFIRDPSKFPDLVHAQRPDPATNLANPAAWWEFVCNNHESLHMAVFLFTDFGTMFDYRSMSGYVSHAYKWVMPDGTWKYVHWFLASDQGPNFEQGNQTREAAPNDSESATRDLYQSLERGECPSWTVKVQVIDPEDAPRLAFNILDVSKHWNLGNYPPDIPVIPERCVGKLTLKKGPENYFEEIEKLAFSPSHLVHGVEPSEDPMLQARLFAYPDAQEHRLGPQFSDMAAKRTGHAANDAPKTKKPAVPLQKQSREHAEWVSQVTSSSWSQPNETDYKFPRELWAALPRLRGEEFQNRLVVNMAESVSQIPEDLRQKVYKTLALVAEDLASRVESLTEEMVVPEQRPRL
Enzyme Length 479
Uniprot Accession Number A8C7R6
Absorption
Active Site ACT_SITE 53; /evidence=ECO:0000250|UniProtKB:P15202
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 1.11.-.-
Enzyme Function FUNCTION: Catalase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:17720822). 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). 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:17720822). However, cloA does not encode a functional enzyme indicating that C.fusiformis terminates its ergot alkaloid pathway at elymoclavine (PubMed:17720822). {ECO:0000250|UniProtKB:Q6ZXC2, ECO:0000269|PubMed:17720822}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000305|PubMed:17720822}.
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (1); Region (2)
Keywords Alkaloid metabolism;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase
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 53,982
Kinetics
Metal Binding METAL 343; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:P15202
Rhea ID
Cross Reference Brenda