| Identification |
| HMDB Protein ID
| HMDBP14168 |
| Secondary Accession Numbers
| None |
| Name
| Ribose-phosphate pyrophosphokinase |
| Synonyms
|
- RPPK
- 5-phospho-D-ribosyl alpha-1-diphosphate
- Phosphoribosyl diphosphate synthase
- Phosphoribosyl pyrophosphate synthase
- P-Rib-PP synthase
- PRPP synthase
- PRPPase
|
| Gene Name
| PRS |
| Protein Type
| Unknown |
| Biological Properties |
| General Function
| Not Available |
| Specific 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). |
| Pathways
|
- 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis
- Biosynthesis of amino acids
- Biosynthesis of secondary metabolites
- Carbon metabolism
- Microbial metabolism in diverse environments
- Pentose phosphate pathway
- Purine metabolism
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| nucleotide biosynthetic process |
| nucleoside metabolic process |
| 5-phosphoribose 1-diphosphate biosynthetic process |
| ribonucleoside monophosphate biosynthetic process |
| Cellular Component |
| cytoplasm |
| Molecular Function |
| magnesium ion binding |
| ATP binding |
| kinase activity |
| ribose phosphate diphosphokinase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
| Number of Residues
| 321 |
| Molecular Weight
| 35207.23 |
| Theoretical pI
| 5.917 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q4L3F7 |
| UniProtKB/Swiss-Prot Entry Name
| KPRS_STAHJ |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
| General References
| - Takeuchi F, Watanabe S, Baba T, Yuzawa H, Ito T, Morimoto Y, Kuroda M, Cui L, Takahashi M, Ankai A, Baba S, Fukui S, Lee JC, Hiramatsu K: Whole-genome sequencing of staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species. J Bacteriol. 2005 Nov;187(21):7292-308. doi: 10.1128/JB.187.21.7292-7308.2005. [PubMed:16237012 ]
|