E3G548 · E3G548_ENTLS

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 site37-39ATP (UniProtKB | ChEBI)
Binding site96-97ATP (UniProtKB | ChEBI)
Binding site131Mg2+ (UniProtKB | ChEBI)
Binding site170Mg2+ (UniProtKB | ChEBI)
Active site194
Binding site196D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site220D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site224-228D-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
    • Ordered locus names
      Entcl_2042

Organism names

Accessions

  • Primary accession
    E3G548

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-121Ribose-phosphate pyrophosphokinase N-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    315
  • Mass (Da)
    34,216
  • Last updated
    2011-01-11 v1
  • Checksum
    4F8E29B118FD6665
MPDMKLFAGNATPELAQRIANRLYTSLGDAAVGRFSDGEVSVQINENVRGGDIFIIQSTCAPTNDNLMELVVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSSVGVDRVLTVDLHAEQIQGFFDVPVDNVFGSPILLEDMLQLNLDNPIVVSPDIGGVVRARAIAKLLNDTDMAIIDKRRPRANVSQVMHIIGDVAGRDCVLVDDMIDTGGTLCKAAEALKERGAKRVFAYATHPIFSGNAANNLRNSVIDEVVVCDTIPLTDEIKALPNVRTLTLSGMLAEAIRRISNEESISAMFEH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002272
EMBL· GenBank· DDBJ
ADO48296.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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