| IED ID | IndEnz0007000444 |
| Enzyme Type ID | catalase000444 |
| Protein Name |
Tryptophan dimethylallyltransferase EC 2.5.1.34 4-dimethylallyltryptophan synthase All-trans-hexaprenyl-diphosphate synthase L-tryptophan dimethylallyl transferase DMATS |
| Gene Name | dmaW fgaPT2 AFUA_2G18040 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MKAANASSAEAYRVLSRAFRFDNEDQKLWWHSTAPMFAKMLETANYTTPCQYQYLITYKECVIPSLGCYPTNSAPRWLSILTRYGTPFELSLNCSNSIVRYTFEPINQHTGTDKDPFNTHAIWESLQHLLPLEKSIDLEWFRHFKHDLTLNSEESAFLAHNDRLVGGTIRTQNKLALDLKDGRFALKTYIYPALKAVVTGKTIHELVFGSVRRLAVREPRILPPLNMLEEYIRSRGSKSTASPRLVSCDLTSPAKSRIKIYLLEQMVSLEAMEDLWTLGGRRRDASTLEGLSLVRELWDLIQLSPGLKSYPAPYLPLGVIPDERLPLMANFTLHQNDPVPEPQVYFTTFGMNDMAVADALTTFFERRGWSEMARTYETTLKSYYPHADHDKLNYLHAYISFSYRDRTPYLSVYLQSFETGDWAVANLSESKVKCQDAACQPTSLPPDLSKTGVYYSGLH |
| Enzyme Length | 459 |
| Uniprot Accession Number | Q50EL0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 89; /note=L-tryptophan; /evidence=ECO:0000269|PubMed:19706516; BINDING 100; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 187; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 189; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 191; /note=L-tryptophan; /evidence=ECO:0000269|PubMed:19706516; BINDING 244; /note=L-tryptophan; /evidence=ECO:0000269|PubMed:19706516; BINDING 257; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 259; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 261; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 343; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 345; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 409; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516; BINDING 413; /note=Substrate; /evidence=ECO:0000269|PubMed:19706516 |
| 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:15870460}; |
| DNA Binding | |
| EC Number | 2.5.1.34 |
| Enzyme Function | FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460, PubMed:23435153). 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:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909). {ECO:0000250|UniProtKB:B6D5I7, ECO:0000269|PubMed:15870460, ECO:0000269|PubMed:15933009, ECO:0000269|PubMed:19672909, ECO:0000269|PubMed:20039019, ECO:0000269|PubMed:20526482, ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:23435153, ECO:0000269|PubMed:26972831}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000269|PubMed:15870460, ECO:0000269|PubMed:23435153}. |
| nucleotide Binding | |
| Features | Beta strand (13); Binding site (13); Chain (1); Erroneous gene model prediction (1); Helix (21); Mutagenesis (6); Natural variant (1); Region (1); Turn (4) |
| Keywords | 3D-structure;Alkaloid metabolism;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996). {ECO:0000269|PubMed:19028996}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3I4X; 3I4Z; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,463 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:15870460}; KM=8 uM for L-tryptophan {ECO:0000269|PubMed:15870460}; Vmax=0.198 umol/min/mg enzyme {ECO:0000269|PubMed:15870460}; |
| Metal Binding | |
| Rhea ID | RHEA:14173 |
| Cross Reference Brenda | 2.5.1.34; |