P9WKE3 · KPRS_MYCTU
- ProteinRibose-phosphate pyrophosphokinase
- Geneprs
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids326 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors (PubMed:22745722).
Catalytic activity
- ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H+
Cofactor
Activity regulation
Activated by inorganic phosphate, and to a lesser extent by sulfate ions (PubMed:21045009, PubMed:21085589).
In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:21045009, PubMed:21085589).
Strongly inhibited by ADP and GDP through competitive binding at the activation site and at a specific allosteric site (PubMed:21045009, PubMed:21085589, PubMed:22745722).
Competitively inhibited by Ca2+, Cu2+ and Fe2+ (PubMed:21045009, PubMed:21085589).
In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:21045009, PubMed:21085589).
Strongly inhibited by ADP and GDP through competitive binding at the activation site and at a specific allosteric site (PubMed:21045009, PubMed:21085589, PubMed:22745722).
Competitively inhibited by Ca2+, Cu2+ and Fe2+ (PubMed:21045009, PubMed:21085589).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8.2 μM | Rib-5-P | |||||
14 μM | Rib-5-P | |||||
25 μM | ATP | |||||
26 μM | CTP | |||||
37 μM | GTP | |||||
52 μM | UTP | |||||
70 μM | Rib-5-P (without divalent cation) |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
601 μmol/min/mg | with ATP as substrate | ||||
530 μmol/min/mg | with Rib-5-P as substrate | ||||
1.41 μmol/min/mg | with Rib-5-P as substrate | ||||
1.12 μmol/min/mg | with ATP as substrate | ||||
0.264 μmol/min/mg | with UTP as substrate | ||||
0.237 μmol/min/mg | with GTP as substrate | ||||
0.237 μmol/min/mg | with CTP as substrate |
kcat is 37 sec-1 with Rib-5-P as substrate (PubMed:21085589).
kcat is 0.83 sec-1 with Rib-5-P as substrate (PubMed:22745722).
kcat is 0.66 sec-1 with ATP as substrate (PubMed:22745722).
kcat is 0.155 sec-1 with UTP as substrate (PubMed:22745722).
kcat is 0.140 sec-1 with GTP as substrate (PubMed:22745722).
kcat is 0.065 sec-1 with CTP as substrate (PubMed:22745722).
kcat is 0.83 sec-1 with Rib-5-P as substrate (PubMed:22745722).
kcat is 0.66 sec-1 with ATP as substrate (PubMed:22745722).
kcat is 0.155 sec-1 with UTP as substrate (PubMed:22745722).
kcat is 0.140 sec-1 with GTP as substrate (PubMed:22745722).
kcat is 0.065 sec-1 with CTP as substrate (PubMed:22745722).
pH Dependence
Optimum pH is close to 8 (PubMed:21085589).
Activities at pH 7 and pH 9.5 are 57% and 70% of the maximal activity, respectively (PubMed:21045009, PubMed:21085589).
Activities at pH 7 and pH 9.5 are 57% and 70% of the maximal activity, respectively (PubMed:21045009, PubMed:21085589).
Temperature Dependence
Thermostable.
Pathway
Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Cell wall biogenesis; cell wall polysaccharide biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 45-47 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NGE | ||||||
Binding site | 104-105 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RQ | ||||||
Binding site | 138 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 178 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 202 | |||||
Sequence: K | ||||||
Binding site | 204 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 230 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 234-238 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DTGGT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | peptidoglycan-based cell wall | |
Cellular Component | plasma membrane | |
Cellular Component | ribose phosphate diphosphokinase complex | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | ribose phosphate diphosphokinase activity | |
Biological Process | 5-phosphoribose 1-diphosphate biosynthetic process | |
Biological Process | capsule polysaccharide biosynthetic process | |
Biological Process | cell wall organization | |
Biological Process | purine nucleotide biosynthetic process | |
Biological Process | ribonucleoside monophosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibose-phosphate pyrophosphokinase
- EC number
- Short namesRPPK
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WKE3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000141164 | 1-326 | Ribose-phosphate pyrophosphokinase | |||
Sequence: MSHDWTDNRKNLMLFAGRAHPELAEQVAKELDVHVTSQDAREFANGEIFVRFHESVRGCDAFVLQSCPAPVNRWLMEQLIMIDALKRGSAKRITAVMPFYPYARQDKKHRGREPISARLIADLLKTAGADRIVTVDLHTDQIQGFFDGPVDHMRGQNLLTGYIRDNYPDGNMVVVSPDSGRVRIAEKWADALGGVPLAFIHKTRDPRVPNQVVSNRVVGDVAGRTCVLIDDMIDTGGTIAGAVALLHNDGAGDVIIAATHGVLSDPAAQRLASCGAREVIVTNTLPIGEDKRFPQLTVLSIAPLLASTIRAVFENGSVTGLFDGDA | ||||||
Cross-link | 29 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length326
- Mass (Da)35,477
- Last updated2014-04-16 v1
- Checksum4CE64D17E783AC37
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP43767.1 EMBL· GenBank· DDBJ | Genomic DNA |