Q97Z86 · KPRS_SACS2

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 site34-36ATP (UniProtKB | ChEBI)
Binding site93-94ATP (UniProtKB | ChEBI)
Binding site127Mg2+ 1 (UniProtKB | ChEBI)
Binding site165Mg2+ 2 (UniProtKB | ChEBI)
Active site188
Binding site190D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site216D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site220-224D-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 Processpurine nucleotide 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
      SSO1045

Organism names

Accessions

  • Primary accession
    Q97Z86

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001412481-291Ribose-phosphate pyrophosphokinase

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    291
  • Mass (Da)
    32,179
  • Last updated
    2002-10-25 v2
  • Checksum
    A18743D629CF60A6
MIIIGGSATNGIDESLSKILSIPLVKVENKIFPDGESYIRVPSSIRDEEVLLVQTTDYPQDKHLIELFLIAETIRDLGAKKLTAIVPYLAYSRQDRRFKDGEAISIKTILHILSEVGVNTLVVVEPHKPEELSYFKGELKIVHPYHQIARKIKEIIEDPFILAPDRGALDRARKIAEEINAPYSYIEKERDRTTGEVRIKEAPNINLKGKDVVIIDDIISTGGTIVQATRLAYSLGAKSVTAAAIHLLLVGGAKERLREVGVKTLIGTNTINVNDKDIITIDVSQSIALSL

Sequence caution

The sequence AAK41307.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE006641
EMBL· GenBank· DDBJ
AAK41307.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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