A0A0F7Q012 · A0A0F7Q012_9LACO
- ProteinRibose-phosphate pyrophosphokinase
- Geneprs
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids322 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic activity
- D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H+
Cofactor
Note: Binds 2 Mg2+ ions per subunit.
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.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 42-44 | ATP (UniProtKB | ChEBI) | |||
Binding site | 135 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 175 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 198 | ||||
Binding site | 225 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | ribose phosphate diphosphokinase complex | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | ribose phosphate diphosphokinase activity | |
Biological Process | 5-phosphoribose 1-diphosphate biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | purine nucleotide 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 > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Ligilactobacillus
Accessions
- Primary accessionA0A0F7Q012
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-125 | Ribose-phosphate pyrophosphokinase N-terminal | |||
Sequence similarities
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)35,187
- Last updated2015-07-22 v1
- Checksum56B1CBF2E954B5F5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011403 EMBL· GenBank· DDBJ | AKI05080.1 EMBL· GenBank· DDBJ | Genomic DNA |