Q8KLK7 · DPGC_STRTO

  • Protein
    (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Activity regulation

Inhibited by DPA-S-(N-acetylcysteamine).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
3.9 μMDPA-CoA
1.7 mMdioxygen
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).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site183substrate
Binding site189substrate
Binding site222-225substrate
Binding site233-238substrate
Binding site296substrate
Binding site325-327substrate
Binding site416substrate

GO annotations

AspectTerm
Molecular Functionidentical protein binding
Molecular Functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Biological Processantibiotic biosynthetic process
Biological Processfatty acid beta-oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
  • EC number

Gene names

    • ORF names
      BU52_01220

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL 15009
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    Q8KLK7

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis189Strong decrease of affinity and the catalytic efficiency compared to the wild-type.
Mutagenesis237Strong 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.
Mutagenesis254Strong decrease of affinity and the catalytic efficiency compared to the wild-type.
Mutagenesis255Same affinity and catalytic efficiency compared to the wild-type.
Mutagenesis299Slight increase of the affinity and 2-fold decrease of the catalytic efficiency compared to the wild-type.
Mutagenesis324Loss of dioxygenase activity.
Mutagenesis425Slight decrease of affinity for DPA-CoA and catalytic efficiency compared to the wild-type. Slight decrease of affinity for dioxygen.
Mutagenesis429Slight decrease of affinity for DPA-CoA and catalytic efficiency compared to the wild-type. Slight decrease of affinity for dioxygen.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004355211-438(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase

Interaction

Subunit

Homohexamer; dimer of trimers.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8KLK7BU52_01220 Q8KLK73EBI-15637670, EBI-15637670

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    438
  • Mass (Da)
    48,174
  • Last updated
    2002-10-01 v1
  • Checksum
    A4C17DCE5E5F3F26
MTTVLPPLEDTDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRFLDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLPQAAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTGEVEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGVRVGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIHKLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLASSDAYFSLPAAKEGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEARLLVDEVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFALMQALRLYGHDVIDKVGRFGGRPPA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U82965
EMBL· GenBank· DDBJ
AAM80546.1
EMBL· GenBank· DDBJ
Genomic DNA
JFCB01000001
EMBL· GenBank· DDBJ
KES08700.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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