P9WKE3 · KPRS_MYCTU

Function

function

Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors (PubMed:22745722).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 Mg2+ ions per subunit (Potential). Can also use Mn2+ (PubMed:21045009, PubMed:21085589).

Activity regulation

Activated by inorganic phosphate, and to a lesser extent by sulfate ions (PubMed:21045009, PubMed:21085589).
In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:21045009, PubMed:21085589).
Strongly inhibited by ADP and GDP through competitive binding at the activation site and at a specific allosteric site (PubMed:21045009, PubMed:21085589, PubMed:22745722).
Competitively inhibited by Ca2+, Cu2+ and Fe2+ (PubMed:21045009, PubMed:21085589).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
8.2 μMRib-5-P
14 μMRib-5-P
25 μMATP
26 μMCTP
37 μMGTP
52 μMUTP
70 μMRib-5-P (without divalent cation)
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
601 μmol/min/mgwith ATP as substrate
530 μmol/min/mgwith Rib-5-P as substrate
1.41 μmol/min/mgwith Rib-5-P as substrate
1.12 μmol/min/mgwith ATP as substrate
0.264 μmol/min/mgwith UTP as substrate
0.237 μmol/min/mgwith GTP as substrate
0.237 μmol/min/mgwith CTP as substrate
kcat is 37 sec-1 with Rib-5-P as substrate (PubMed:21085589).
kcat is 0.83 sec-1 with Rib-5-P as substrate (PubMed:22745722).
kcat is 0.66 sec-1 with ATP as substrate (PubMed:22745722).
kcat is 0.155 sec-1 with UTP as substrate (PubMed:22745722).
kcat is 0.140 sec-1 with GTP as substrate (PubMed:22745722).
kcat is 0.065 sec-1 with CTP as substrate (PubMed:22745722).

pH Dependence

Optimum pH is close to 8 (PubMed:21085589).
Activities at pH 7 and pH 9.5 are 57% and 70% of the maximal activity, respectively (PubMed:21045009, PubMed:21085589).

Temperature Dependence

Thermostable.

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.
Cell wall biogenesis; cell wall polysaccharide biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site45-47ATP (UniProtKB | ChEBI)
Binding site104-105ATP (UniProtKB | ChEBI)
Binding site138Mg2+ 1 (UniProtKB | ChEBI)
Binding site178Mg2+ 2 (UniProtKB | ChEBI)
Active site202
Binding site204D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site230D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site234-238D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentpeptidoglycan-based cell wall
Cellular Componentplasma membrane
Cellular Componentribose phosphate diphosphokinase complex
Molecular FunctionATP binding
Molecular Functionkinase activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionribose phosphate diphosphokinase activity
Biological Process5-phosphoribose 1-diphosphate biosynthetic process
Biological Processcapsule polysaccharide biosynthetic process
Biological Processcell wall organization
Biological Processpurine nucleotide biosynthetic process
Biological Processribonucleoside monophosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribose-phosphate pyrophosphokinase
  • EC number
  • Short names
    RPPK
  • Alternative names
    • 5-phospho-D-ribosyl alpha-1-diphosphate synthase
    • Phosphoribosyl diphosphate synthase
    • Phosphoribosyl pyrophosphate synthase
      (P-Rib-PP synthase
      ; PRPP synthase
      ; PRPPase
      )

Gene names

    • Name
      prs
    • Synonyms
      prsA
    • ORF names
      MTCY10G2.32
    • Ordered locus names
      Rv1017c

Organism names

Accessions

  • Primary accession
    P9WKE3
  • Secondary accessions
    • L0T8D7
    • P65232
    • P96383

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, cross-link.

TypeIDPosition(s)Description
ChainPRO_00001411641-326Ribose-phosphate pyrophosphokinase
Cross-link29Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Keywords

Proteomic databases

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    326
  • Mass (Da)
    35,477
  • Last updated
    2014-04-16 v1
  • Checksum
    4CE64D17E783AC37
MSHDWTDNRKNLMLFAGRAHPELAEQVAKELDVHVTSQDAREFANGEIFVRFHESVRGCDAFVLQSCPAPVNRWLMEQLIMIDALKRGSAKRITAVMPFYPYARQDKKHRGREPISARLIADLLKTAGADRIVTVDLHTDQIQGFFDGPVDHMRGQNLLTGYIRDNYPDGNMVVVSPDSGRVRIAEKWADALGGVPLAFIHKTRDPRVPNQVVSNRVVGDVAGRTCVLIDDMIDTGGTIAGAVALLHNDGAGDVIIAATHGVLSDPAAQRLASCGAREVIVTNTLPIGEDKRFPQLTVLSIAPLLASTIRAVFENGSVTGLFDGDA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP43767.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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