Hmdb loader
Identification
HMDB Protein ID HMDBP14168
Secondary Accession Numbers None
Name Ribose-phosphate pyrophosphokinase
Synonyms
  1. RPPK
  2. 5-phospho-D-ribosyl alpha-1-diphosphate
  3. Phosphoribosyl diphosphate synthase
  4. Phosphoribosyl pyrophosphate synthase
  5. P-Rib-PP synthase
  6. PRPP synthase
  7. 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
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
  1. 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 ]