Q8KLK7 · DPGC_STRTO
- Protein(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids438 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester bond to generate free CoA (PubMed:17507985, PubMed:18004875).
DpgC has the ability to process a diverse range of substituted phenylacetyl-CoA substrates (PubMed:18004875).
DpgC has the ability to process a diverse range of substituted phenylacetyl-CoA substrates (PubMed:18004875).
Catalytic activity
- (3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA + H+
Activity regulation
Inhibited by DPA-S-(N-acetylcysteamine).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.9 μM | DPA-CoA | |||||
1.7 mM | dioxygen |
kcat is 10.32 min-1 for dioxygenase activity with DPA-CoA as substrate (PubMed:18004875).
kcat is 0.172 sec-1 for dioxygenase activity with DPA-CoA as substrate (PubMed:17507985).
kcat is 0.172 sec-1 for dioxygenase activity with DPA-CoA as substrate (PubMed:17507985).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 183 | substrate | ||||
Sequence: D | ||||||
Binding site | 189 | substrate | ||||
Sequence: E | ||||||
Binding site | 222-225 | substrate | ||||
Sequence: HPRY | ||||||
Binding site | 233-238 | substrate | ||||
Sequence: AGINLK | ||||||
Binding site | 296 | substrate | ||||
Sequence: G | ||||||
Binding site | 325-327 | substrate | ||||
Sequence: IPG | ||||||
Binding site | 416 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | identical protein binding | |
Molecular Function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen | |
Biological Process | antibiotic biosynthetic process | |
Biological Process | fatty acid beta-oxidation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionQ8KLK7
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 189 | Strong decrease of affinity and the catalytic efficiency compared to the wild-type. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 237 | Strong decrease of affinity for DPA-CoA and 2-fold decrease of the catalytic efficiency compared to the wild-type. Slight decrease of affinity for dioxygen. | ||||
Sequence: L → T | ||||||
Mutagenesis | 254 | Strong decrease of affinity and the catalytic efficiency compared to the wild-type. | ||||
Sequence: R → K | ||||||
Mutagenesis | 255 | Same affinity and catalytic efficiency compared to the wild-type. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 299 | Slight increase of the affinity and 2-fold decrease of the catalytic efficiency compared to the wild-type. | ||||
Sequence: Q → N | ||||||
Mutagenesis | 324 | Loss of dioxygenase activity. | ||||
Sequence: I → T | ||||||
Mutagenesis | 425 | Slight decrease of affinity for DPA-CoA and catalytic efficiency compared to the wild-type. Slight decrease of affinity for dioxygen. | ||||
Sequence: V → T | ||||||
Mutagenesis | 429 | Slight decrease of affinity for DPA-CoA and catalytic efficiency compared to the wild-type. Slight decrease of affinity for dioxygen. | ||||
Sequence: V → T |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435521 | 1-438 | (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase | |||
Sequence: MTTVLPPLEDTDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRFLDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLPQAAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTGEVEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGVRVGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIHKLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLASSDAYFSLPAAKEGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEARLLVDEVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFALMQALRLYGHDVIDKVGRFGGRPPA |
Interaction
Subunit
Homohexamer; dimer of trimers.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8KLK7 | BU52_01220 Q8KLK7 | 3 | EBI-15637670, EBI-15637670 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length438
- Mass (Da)48,174
- Last updated2002-10-01 v1
- ChecksumA4C17DCE5E5F3F26
Keywords
- Technical term