A0AAQ0FGQ2 · A0AAQ0FGQ2_BURCE

Function

function

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.

Activity regulation

Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.

Pathway

Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site18-20substrate
Binding site46-50substrate
Binding site147substrate
Binding site192ATP (UniProtKB | ChEBI)
Binding site228-233ATP (UniProtKB | ChEBI)
Binding site255K+ (UniProtKB | ChEBI)
Binding site257K+ (UniProtKB | ChEBI)
Binding site260-261ATP (UniProtKB | ChEBI)
Active site261Proton acceptor
Binding site261substrate
Binding site291K+ (UniProtKB | ChEBI)
Binding site294K+ (UniProtKB | ChEBI)
Binding site296K+ (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functiontransferase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • Name
      rbsK
    • ORF names
      DPR02_17370

Organism names

  • Taxonomic identifier
  • Strain
    • PT02
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex

Accessions

  • Primary accession
    A0AAQ0FGQ2

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-303Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    309
  • Mass (Da)
    30,293
  • Last updated
    2024-10-02 v1
  • MD5 Checksum
    27CE2C1B8C10BD1D7B9C1CA874A6A4AC
MTAPVAGAGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSASASTGVALIVVDDASQNAIVIVAGGNGEVTTDTVARHEAALASADVVICQLETPPDAVFAALSAGRRLGRTVVLNPAPAIAPLPDGWLPLVDYLIPNEVEAAALTALPVRDPAEAEAAARALQAGGARNVLVTLGARGVLALTADGVARHYPAPAVQAVDTTAAGDTFIGGFSARLAAGADVDTAIRFAQRAAALSVTRAGAQPSIPTLAELAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QLUZ01000009
EMBL· GenBank· DDBJ
RAQ08653.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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