A0A2S5DNN0 · A0A2S5DNN0_9BURK
- ProteinDeoxyribokinase
- GenerbsK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent phosphorylation of 2-deoxy-D-ribose to 2-deoxy-D-ribose 5-phosphate (dRib-5P), allowing the use of deoxyribose as the sole carbon source.
Catalytic activity
- 2-deoxy-D-ribose + ATP = 2-deoxy-D-ribose 5-phosphate + ADP + H+
Cofactor
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 11 | Important for substrate specificity | |||
Binding site | 11-13 | substrate | |||
Binding site | 39-43 | substrate | |||
Binding site | 140 | substrate | |||
Binding site | 185 | ATP (UniProtKB | ChEBI) | |||
Binding site | 221-226 | ATP (UniProtKB | ChEBI) | |||
Binding site | 247 | K+ (UniProtKB | ChEBI) | |||
Binding site | 249 | K+ (UniProtKB | ChEBI) | |||
Binding site | 252-253 | ATP (UniProtKB | ChEBI) | |||
Active site | 253 | Proton acceptor | |||
Binding site | 253 | substrate | |||
Binding site | 283 | K+ (UniProtKB | ChEBI) | |||
Binding site | 286 | K+ (UniProtKB | ChEBI) | |||
Binding site | 288 | K+ (UniProtKB | ChEBI) | |||
Binding site | 292 | K+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | ribokinase activity | |
Biological Process | D-ribose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDeoxyribokinase
- EC number
- Short namesdRK
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A2S5DNN0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)32,320
- Last updated2018-07-18 v1
- Checksum067D26B1261ECA99
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PQVP01000003 EMBL· GenBank· DDBJ | POZ80662.1 EMBL· GenBank· DDBJ | Genomic DNA |