Q9ZGH6 · DESVI_STRVZ
- ProteindTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
- GenedesVI
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of desosamine, found in certain macrolide antibiotics such as erthyromycin, azithromycin, clarithromycin, and methymycin. Catalyzes the last step in the biosynthesis of dTDP-desosamine, i.e. the N,N-dimethylation of the 3-amino group of dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose.
Catalytic activity
- dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-desosamine + 2 H+ + 2 S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
307.4 μM | dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose | |||||
276.6 μM | dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose |
kcat is 92 min-1 with dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose as substrate. kcat is 4.2 min-1 with dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose as substrate.
Pathway
Antibiotic biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14 | substrate | ||||
Sequence: Y | ||||||
Binding site | 17 | substrate | ||||
Sequence: R | ||||||
Binding site | 21 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 46 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 67 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 89-90 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DM | ||||||
Binding site | 105 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 145-147 | substrate | ||||
Sequence: TFA | ||||||
Binding site | 152 | substrate | ||||
Sequence: S | ||||||
Binding site | 165-169 | substrate | ||||
Sequence: RVSHS | ||||||
Binding site | 229 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | protein homodimerization activity | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | antibiotic biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namedTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionQ9ZGH6
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000418452 | 1-237 | dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose N,N-dimethyltransferase | |||
Sequence: MYEVDHADVYDLFYLGRGKDYAAEASDIADLVRSRTPEASSLLDVACGTGTHLEHFTKEFGDTAGLELSEDMLTHARKRLPDATLHQGDMRDFRLGRKFSAVVSMFSSVGYLKTTEELGAAVASFAEHLEPGGVVVVEPWWFPETFADGWVSADVVRRDGRTVARVSHSVREGNATRMEVHFTVADPGKGVRHFSDVHLITLFHQAEYEAAFTAAGLRVEYLEGGPSGRGLFVGVPA |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length237
- Mass (Da)25,979
- Last updated1999-05-01 v1
- Checksum156E67A0E7406AE8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF079762 EMBL· GenBank· DDBJ | AAC68678.1 EMBL· GenBank· DDBJ | Genomic DNA |