| IED ID | IndEnz0007000077 |
| Enzyme Type ID | catalase000077 |
| Protein Name |
Tryptophan dimethylallyltransferase EC 2.5.1.34 4-dimethylallyltryptophan synthase DMATS All-trans-hexaprenyl-diphosphate synthase L-tryptophan dimethylallyl transferase |
| Gene Name | dmaW |
| 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 | MMTKAPATAVYDTLSLLFDFPNQEQRLWWHSIAPMFAAMLDTAGHNVHDQYRHLGIFKKHIIPFLGVYPAQGKHTWPSVLTRYGIPFELSLNCLDSVVRYTFEPTTEHTGTGDDSYNAFAILECIQKLVRIQPGIDMEWFSYFRNELVLNATESARLGRNDSVNQQPIRTQNKLALDLKGDRFALKVYLYPHLKSIATGVSSHDLIFNSVRKLSQKHTSIQPSFNVLCDYVASRNDPDSNAAEAEAGVPASALRARLLSCDLVDPSKSRIKIYLLEQTVSLTAMEDLWTLGGRRTDSSTLNGLDMMRELWHLLQIPSGFMKYPESDLKLGEVPDEQLPSMVHYALHPDQPMPEPQVYFTVFGMSDAGITNALATFFSRHGWYEMAKKYRVFLEGSFPNHDFESLNYLHTYVSFSYRKNKPYLSVYLHSFETGQWPAFSDDPTAFNAFKRCDLSLT |
| Enzyme Length | 455 |
| Uniprot Accession Number | Q12594 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 88; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 99; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 186; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 188; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 190; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 256; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 269; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 271; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 273; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 355; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 357; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 421; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 425; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912, ChEBI:CHEBI:58209; EC=2.5.1.34; Evidence={ECO:0000269|PubMed:1605639, ECO:0000269|PubMed:7488077}; |
| DNA Binding | |
| EC Number | 2.5.1.34 |
| Enzyme Function | FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:7488077, PubMed:17720822, PubMed:1605639). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:7488077, PubMed:1605639). 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:P0CT20, ECO:0000269|PubMed:1605639, ECO:0000269|PubMed:17720822, ECO:0000269|PubMed:7488077}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000269|PubMed:1605639, ECO:0000269|PubMed:7488077}. |
| nucleotide Binding | |
| Features | Binding site (13); Chain (1); Region (1) |
| Keywords | Alkaloid metabolism;Direct protein sequencing;Transferase |
| 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 | 51,858 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for dimethylallyl diphosphate (in metal-free EDTA buffer) {ECO:0000269|PubMed:1605639}; KM=40 uM for L-tryptophan (in metal-free EDTA buffer) {ECO:0000269|PubMed:1605639}; KM=8 uM for dimethylallyl diphosphate (in the presence of 4 mM Ca(2+)) {ECO:0000269|PubMed:1605639}; KM=17 uM for L-tryptophan (in the presence of 4 mM Ca(2+)) {ECO:0000269|PubMed:1605639}; KM=8 uM for dimethylallyl diphosphate (in the presence of 4 mM Mg(2+)) {ECO:0000269|PubMed:1605639}; KM=12 uM for L-tryptophan (in the presence of 4 mM Mg(2+)) {ECO:0000269|PubMed:1605639}; Vmax=215 nmol/min/mg enzyme (in metal-free EDTA buffer) {ECO:0000269|PubMed:1605639}; Vmax=504 nmol/min/mg enzyme (in the presence of 4 mM Ca(2+)) {ECO:0000269|PubMed:1605639}; Vmax=455 nmol/min/mg enzyme (in the presence of 4 mM Mg(2+)) {ECO:0000269|PubMed:1605639}; |
| Metal Binding | |
| Rhea ID | RHEA:14173 |
| Cross Reference Brenda |