| IED ID | IndEnz0007000050 |
| Enzyme Type ID | catalase000050 |
| Protein Name |
Tryptophan dimethylallyltransferase cnsF EC 2.5.1.34 4-dimethylallyltryptophan synthase DMATS All-trans-hexaprenyl-diphosphate synthase Communesin biosynthesis cluster protein F L-tryptophan dimethylallyl transferase |
| Gene Name | cnsF PEX2_055400 |
| Organism | Penicillium expansum (Blue mold rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium expansum (Blue mold rot fungus) |
| Enzyme Sequence | MGTHDMSPNASHSYIYRVLSDILEFPDNEQRMWWHSVAPMFAEMLRACGYDIHEQYKILGIWKKAVIPFLGCYPTNDGPRWLSILTRYGTPFELSLNCSHRLVRYTFEPINAATGTDKDPFNTQAIWESLSQLRRLNGDVDTELFNHFKANLTVDNAESAHLVESNLAGSKIRTQNKLALDLQNGSFVVKAYFYPTLKSAATGRSITDLMLSSVRQQVQKWSPTLAQPLSVLEEYIEARGPDSTASPRLLSCDLINPERARTKIYLLERQVSIEAMEDLWTLGGRRKSDSALAALDIIREIWSLIQLPPCLASYPSGYLPLGTVPDEQLPLMVNYTLRPDDPMPEPQVYFTTFGQNDLHVTNALTAFFERQGWTELAESYKENLRAYYPHADQETANYIHAYVSFSYRKGVSYMSVYLQTLETGDWPITYSPKRQYLCNEHPIHLKELAKACA |
| Enzyme Length | 453 |
| Uniprot Accession Number | A0A0A2JWD0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 93; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 104; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 190; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 192; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 194; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 248; /note=L-tryptophan; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 261; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 263; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 265; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 347; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q50EL0; BINDING 349; /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:25571861}; |
| DNA Binding | |
| EC Number | 2.5.1.34 |
| Enzyme Function | FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of communesins, a prominent class of indole alkaloids with great potential as pharmaceuticals (PubMed:25571861). Communesins are biosynthesized by the coupling of tryptamine and aurantioclavine, two building blocks derived from L-tryptophan (PubMed:25571861). The L-tryptophan decarboxylase cnsB converts L-tryptophan to tryptamine, whereas the tryptophan dimethylallyltransferase cnsF converts L-tryptophan to 4-dimethylallyl tryptophan which is further transformed to aurantioclavine by the aurantioclavine synthase cnsA, probably aided by the catalase cnsD (PubMed:25571861). The cytochrome P450 monooxygenase cnsC catalyzes the heterodimeric coupling between the two different indole moieties, tryptamine and aurantioclavine, to construct vicinal quaternary stereocenters and yield the heptacyclic communesin scaffold (PubMed:26963294). The O-methyltransferase cnsE then methylates the communesin scaffold to produce communesin K, the simplest characterized communesin that contains the heptacyclic core (PubMed:25571861). The dioxygenase cnsJ converts communesin K into communesin I (PubMed:25571861). Acylation to introduce the hexadienyl group at position N16 of communesin I by the acyltransferase cnsK leads to the production of communesin B. The hexadienyl group is produced by the highly reducing polyketide synthase cnsI, before being hydrolytically removed from cnsI by the serine hydrolase cnsH, converted into hexadienyl-CoA by the CoA ligase cnsG, and then transferred to communesin I by cnsK (PubMed:25571861). Surprisingly, cnsK may also be a promiscuous acyltransferase that can tolerate a range of acyl groups, including acetyl-, propionyl-, and butyryl-CoA, which lead to communesins A, G and H respectively (PubMed:25571861). The roles of the alpha-ketoglutarate-dependent dioxygenases cnsM and cnsP have still to be determined (PubMed:25571861). {ECO:0000269|PubMed:25571861, ECO:0000269|PubMed:26963294}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25571861}. |
| nucleotide Binding | |
| Features | Binding site (11); Chain (1); Region (1) |
| Keywords | Reference proteome;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 | 51,691 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14173 |
| Cross Reference Brenda |