Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A951H804 · A0A951H804_UNCAB

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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
IDPosition(s)Description
Binding site75-77ATP (UniProtKB | ChEBI)
Binding site134-135ATP (UniProtKB | ChEBI)
Binding site168Mg2+ (UniProtKB | ChEBI)
Binding site209Mg2+ (UniProtKB | ChEBI)
Active site232
Binding site234D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site258D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site262-266D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentribose phosphate diphosphokinase complex
Molecular FunctionATP binding
Molecular Functionkinase activity
Molecular Functionmagnesium ion binding
Molecular Functionribose phosphate diphosphokinase activity
Biological Process5-phosphoribose 1-diphosphate biosynthetic process
Biological Processphosphorylation
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
    • ORF names
      JO316_01510

Organism names

  • Taxonomic identifier
  • Strain
    • CP_BM_RX_R8_36
  • Taxonomic lineage
    Bacteria > Abditibacteriota > Abditibacteriia > Abditibacteriales > Abditibacteriaceae

Accessions

  • Primary accession
    A0A951H804

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain42-158Ribose-phosphate pyrophosphokinase N-terminal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    353
  • Mass (Da)
    38,194
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    B92F0DCCC075C13D76CD6F0392A4E878
MPSKPNCAPKECVAVKETLETLDYSVAPHLNGHAPEADLSGLKIFSGNSNLPLAHAIADCLDKPLGSMTTRRFADGEMHCAINESIRGADVFIIQPTCGPVNDTLMELLIMCDAFKRASARRIVPIMPYFGYARQDKKIRPREPISAKLVSDLITLAGADRIFAIDLHAGQIQGFFDRPVDHLPAQPIIANYLIKKGIFDHNVTVVSPDVGAVGRATILAERLGADLAIVAKRRPEPGKVKVIDVIGDVKNRVCVLIDDMIDSGGTFMAAAHELMERGAQEVYACATHPVLSGEAVGRIQESAIKELVVTDTIPIPPERMIPKITVLSVAAVCAQAICRIHNDESVSTMFESF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAFAZH010000004
EMBL· GenBank· DDBJ
MBV9864007.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help