A5VJ52 · A5VJ52_LIMRD

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

Lacks conserved residue(s) required for the propagation of feature annotation.
Part of a set of proteins in which some residues (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved.

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.

TypeIDPosition(s)Description
Binding site43-45ATP (UniProtKB | ChEBI)
Binding site102-103ATP (UniProtKB | ChEBI)
Binding site136Mg2+ (UniProtKB | ChEBI)
Binding site176Mg2+ (UniProtKB | ChEBI)
Binding site229D-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
    Putative 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
      Lreu_0609

Organism names

Accessions

  • Primary accession
    A5VJ52

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-123Ribose-phosphate pyrophosphokinase N-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    324
  • Mass (Da)
    36,060
  • Last updated
    2007-07-10 v1
  • Checksum
    D0EC229F948E9F43
MTQIKNADNVRLFSLNSNPKLAEQISQRVGIPLSKASISHFADGEIKITIDESIRGCEVYVIQSVSDPVNTNLMELLIMVDALRRASAAKINVVMPYYGYARQDRKARSREPITAKLIANLLEMDQISRLVTIDLHAPQVQGFFDIPVDHLQATSLFTKYIEEQNLGDDIVVVAPDHAGVNLARKYAERIKASIAIIDNRNDEVRERTEQEVPEYVIGDVKGKTAIIVDDIVDTGVRMNLSAQALKNFGAAKVYGIATHAVLSADAVNTLQNSPLEKMIVTDTIQLPKEKEFSKLVQLSVDDLLKEAIVRIHNNQSIDTLFNRK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000705
EMBL· GenBank· DDBJ
ABQ82876.1
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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