A0A380GBU9 · A0A380GBU9_STAIN

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

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.

TypeIDPosition(s)Description
Binding site44-46ATP (UniProtKB | ChEBI)
Binding site103-104ATP (UniProtKB | ChEBI)
Binding site137Mg2+ (UniProtKB | ChEBI)
Binding site179Mg2+ (UniProtKB | ChEBI)
Active site202
Binding site204D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site228D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site232-236D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionguanine phosphoribosyltransferase activity
Molecular Functionhypoxanthine phosphoribosyltransferase activity
Molecular Functionkinase activity
Molecular Functionmagnesium ion binding
Molecular Functionribose phosphate diphosphokinase activity
Biological Process5-phosphoribose 1-diphosphate biosynthetic process
Biological Processnucleotide 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
      NCTC11048_02923

Organism names

Accessions

  • Primary accession
    A0A380GBU9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-127Ribose-phosphate pyrophosphokinase N-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    321
  • Mass (Da)
    35,293
  • Last updated
    2018-11-07 v1
  • Checksum
    9C5787763C12300A
MLNTEYKNSSLKIFSLKGNEPLAQEVADHVGVELGKCTVKRFSDGEIQINIEESIRGCDVFIIQPTSNPVNVHLMELLIMIDACKRASAANITIVVPYYGYARQDRKARSREPITAKLVADLFETAGADRMIALDLHAPQIQGFFDIPIDHLMGVPILAEYFLNNEEIDPENCVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGEIEGRTAIIIDDIIDTAGTITLAAQALKDKGATKVFACCTHPVLSGPAKERIENSAIQELVVTNSIQLNEEQKPNNIVELSVAELLAQAIVRVYERESVSVLFD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UHDP01000003
EMBL· GenBank· DDBJ
SUM47820.1
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.
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