D1D8L6 · CDNTP_ASPFM
- ProteinCyclic dipeptide prenyltransferase
- GenecdpNPT
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids440 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Prenyltransferase that catalyzes reverse prenylation at position N-1 of tryptophan-containing cyclic dipeptides (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141).
Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate specificities toward its aromatic substrates (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141).
Shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009).
Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate specificities toward its aromatic substrates (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141).
Shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009).
Catalytic activity
- dimethylallyl diphosphate + harmol = 6-(3-dimethylallyl)harmol + diphosphateThis reaction proceeds in the forward direction.
- (R)-benzodiazepinedione + dimethylallyl diphosphate = (2S,3R,11R)-aszonalenin + diphosphateThis reaction proceeds in the forward direction.
- (S)-benzodiazepinedione + dimethylallyl diphosphate = (2S,3R,11S)-aszonalenin + diphosphateThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
650 μM | dimethylallyl diphosphate (DMAPP) | |||||
300 μM | H-L-Trp-L-Gly-OH | for aminopeptidase activity | ||||
380 μM | L-tryptophan | |||||
128 μM | cyclo-D-Trp-L-Tyr |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 108 | substrate | ||||
Sequence: T | ||||||
Binding site | 116 | substrate | ||||
Sequence: E | ||||||
Binding site | 129 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 219 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 221 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 223 | substrate | ||||
Sequence: F | ||||||
Binding site | 286 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 288 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 366 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 431 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 435 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aminopeptidase activity | |
Molecular Function | prenyltransferase activity | |
Biological Process | alkaloid metabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCyclic dipeptide prenyltransferase
- EC number
- Short namesCdpNPT
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionD1D8L6
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 108 | Decreases the enzymatic activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 131 | Does not significantly affect the enzymatic activity. | ||||
Sequence: A → G | ||||||
Mutagenesis | 131 | Strongly decreases the enzymatic activity. | ||||
Sequence: A → V |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456714 | 1-440 | Cyclic dipeptide prenyltransferase | |||
Sequence: MDGEMTASPPDISACDTSAVDEQTGQSGQSQAPIPKDIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEYLCLFAQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAFEPVRYQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAKDERNLNEEQLTKYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATGQTGSNACFGAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAHTRFKVYIADPLVTLARAEEHWTLGGRLTDEDAAVGLEIIRGLWSELGIIQGPLEPSAMMEKGLLPIMLNYEMKAGQRLPKPKLYMPLTGIPETKIARIMTAFFQRHDMPEQAEVFMENLQAYYEGKNLEEATRYQAWLSFAYTKEKGPYLSIYYFWPE |
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MDGEMTASPPDISACDTSAVDEQTGQSGQSQAP | ||||||
Compositional bias | 11-33 | Polar residues | ||||
Sequence: DISACDTSAVDEQTGQSGQSQAP |
Sequence similarities
Belongs to the tryptophan dimethylallyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length440
- Mass (Da)49,681
- Last updated2010-01-19 v1
- ChecksumC42AB2ACA57CE244
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-33 | Polar residues | ||||
Sequence: DISACDTSAVDEQTGQSGQSQAP |
Keywords
- Technical term