D2Z030 · DCSG_STRLA
- ProteinCycloserine biosynthesis protein DcsG
- GenedcsG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids299 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the synthesis of D-cycloserine from O-ureido-D-serine (D-OUS). It reacts with D-OUS, D-homocysteine and beta-aminooxy-D-alanine.
Catalytic activity
- ATP + H+ + H2O + O-ureido-D-serine = ADP + CO2 + D-cycloserine + NH4+ + phosphate
Cofactor
Note: Binds 2 Mg2+ ions per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.3 mM | O-ureido-D-serine (D-OUS) | |||||
10 mM | D-OUS in the presence of 5 mM ATP | |||||
19 mM | D-homocysteine | |||||
73 μM | ATP, in the presence of 50 mM D-OUS |
kcat is 2200 sec-1 with D-OUS as substrate. kcat is 0.86 sec-1 with D-homocysteine as substrate.
pH Dependence
Optimum pH is 8.0.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 92 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 137 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 144 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 175 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 176 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 178 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Active site | 220 | |||||
Sequence: R | ||||||
Active site | 254 | |||||
Sequence: R | ||||||
Binding site | 269 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 269 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 271 | |||||
Sequence: E | ||||||
Binding site | 271 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | cyclo-ligase activity | |
Molecular Function | metal ion binding | |
Biological Process | antibiotic biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCycloserine biosynthesis protein DcsG
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionD2Z030
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene do not produce cycloserine (DCS).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 57 | Loss of enzyme activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 142 | About 80% activity on D-OUS, 40% on D-homocysteine and beta-aminooxy-D-alanine. | ||||
Sequence: C → A | ||||||
Mutagenesis | 143 | About 15% activity on D-OUS, 5% on D-homocysteine and 30% on beta-aminooxy-D-alanine. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 202 | Nearly complete loss of activity on all substrates. | ||||
Sequence: K → A | ||||||
Mutagenesis | 215 | About 5% activity on D-OUS and beta-aminooxy-D-alanine, nearly complete loss of activity on D-homocysteine. | ||||
Sequence: P → A | ||||||
Mutagenesis | 220 | Nearly complete loss of activity on D-OUS, about 5% activity on D-homocysteine and beta-aminooxy-D-alanine. | ||||
Sequence: R → A | ||||||
Mutagenesis | 254 | Nearly complete loss of activity on all substrates. | ||||
Sequence: R → A | ||||||
Mutagenesis | 271 | Nearly complete loss of activity on all substrates. | ||||
Sequence: E → A or Q | ||||||
Mutagenesis | 276 | About 5% activity on D-OUS, 50% on D-homocysteine and 20% beta-aminooxy-D-alanine. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000424059 | 1-299 | Cycloserine biosynthesis protein DcsG | |||
Sequence: MGILALVTDAVSLPIDYDMPPLLEACRTVGITAEVCDWEDGTVDWSRFEAVVFRSPWTWAERQAEFLAFCERVSHVTRLITPMPLVRWALDKRYLADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLKP |
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 95-298 | ATP-grasp | ||||
Sequence: LADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLK |
Family and domain databases
Sequence
- Sequence statusComplete
- Length299
- Mass (Da)32,786
- Last updated2010-03-23 v1
- Checksum8E4784DF256B9B23
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB516431 EMBL· GenBank· DDBJ | BAI70381.1 EMBL· GenBank· DDBJ | Genomic DNA |