K0JRN3 · K0JRN3_SACES

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 site42-44ATP (UniProtKB | ChEBI)
Binding site101-102ATP (UniProtKB | ChEBI)
Binding site135Mg2+ (UniProtKB | ChEBI)
Binding site175Mg2+ (UniProtKB | ChEBI)
Active site199
Binding site201D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site227D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site231-235D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
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
    • Ordered locus names
      BN6_07140

Organism names

Accessions

  • Primary accession
    K0JRN3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-125Ribose-phosphate pyrophosphokinase N-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    323
  • Mass (Da)
    35,358
  • Last updated
    2012-11-28 v1
  • Checksum
    CF7C1AFD472FE95F
MPGTPKKNLMLFGGRAYPELTEQVAKHLNVSVTPQSAYDFANGEIFVRFEESVRGCDAFVIQSHCAPINQWLMEHLIMVDALKRASAKRITVIMPFYPYARQDKKHRGREPISARLVADLFKTAGADRLVAVDLHTAQIQGFFDGPVDHLWAMPLLAEHIRDKYAGRDITVVSPDAGRTKLAEKWADTLGGTPIAFIHKTRDPLRPNEVVANRVVGEVKGRLCVVIDDMIDTGGTITKAVDQLLAEGASDVVIAATHPVLSGPAVERLQACGAREVVFTDTLPIPAEKRFDAMTVLPIAPLLARVIQEVFEDGSVTSLFDGNA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HE804045
EMBL· GenBank· DDBJ
CCH28042.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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