A0A290S4N7 · A0A290S4N7_9GAMM
- ProteinRibose-phosphate pyrophosphokinase
- GeneprsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids315 (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
- ATP + D-ribose 5-phosphate = 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 | 37-39 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DGE | ||||||
Binding site | 96-97 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RQ | ||||||
Binding site | 131 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 170 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 194 | |||||
Sequence: K | ||||||
Binding site | 196 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 220 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224-228 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DTGGT |
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 | 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 > Pseudomonadota > Gammaproteobacteria > Alteromonadales > Pseudoalteromonadaceae > Pseudoalteromonas
Accessions
- Primary accessionA0A290S4N7
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-121 | Ribose-phosphate pyrophosphokinase N-terminal | ||||
Sequence: MKLFAGNATPELAQKVAKRLYIELGDAVVGRFSDGEISVQINENVRGSDVFILQSTCAPTNDNLMELIVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSSVG |
Sequence similarities
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)34,505
- Last updated2017-12-20 v1
- ChecksumB9C8BBAA5022BCB3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011025 EMBL· GenBank· DDBJ | ATC87134.1 EMBL· GenBank· DDBJ | Genomic DNA |