A0A498H2F0 · A0A498H2F0_9EURY
- ProteinRibose-phosphate pyrophosphokinase
- Geneprs
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids282 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 34-36 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DGE | ||||||
Binding site | 86-87 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RQ | ||||||
Binding site | 119 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 158 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 181 | |||||
Sequence: K | ||||||
Binding site | 183 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 207 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211-215 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: STGGT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 | 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
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanomicrobiales > Methanomicrobiaceae > Methanoculleus
Accessions
- Primary accessionA0A498H2F0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-107 | Ribose-phosphate pyrophosphokinase N-terminal | ||||
Sequence: MKIISTERSQVLAARVSEITGYQLLDTKFNRFPDGELYLRTGETDEETIIVSSVVDNDALVQTLLAIDACDSSRITLVLPYLGYARQDKRFTAGEPISARAVARALS | ||||||
Domain | 125-239 | Phosphoribosyltransferase | ||||
Sequence: QYFDAPATNISIAPAIGGYIRELGVRNPLILAPDDGAAAFAAEVAAVGGWDTDHLEKTRLSGDTVRMEPKSLPAASREVVIVDDIISTGGTLATAAGMLYGQGATAIHAVCVHGV |
Sequence similarities
Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length282
- Mass (Da)29,713
- Last updated2019-06-05 v1
- Checksum14A98B163E9EEC0A
Keywords
- Technical term