A0A9X1K3Z2 · A0A9X1K3Z2_9ENTR

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.

TypeIDPosition(s)Description
Binding site14-16substrate
Binding site42-46substrate
Binding site143substrate
Binding site187ATP (UniProtKB | ChEBI)
Binding site223-228ATP (UniProtKB | ChEBI)
Binding site249K+ (UniProtKB | ChEBI)
Binding site251K+ (UniProtKB | ChEBI)
Binding site254-255ATP (UniProtKB | ChEBI)
Active site255Proton acceptor
Binding site255substrate
Binding site279ATP (UniProtKB | ChEBI)
Binding site285K+ (UniProtKB | ChEBI)
Binding site288K+ (UniProtKB | ChEBI)
Binding site290K+ (UniProtKB | ChEBI)
Binding site294K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • Name
      rbsK
    • ORF names
      CTBON28M_04715

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • On28M
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter

Accessions

  • Primary accession
    A0A9X1K3Z2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-297Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    309
  • Mass (Da)
    32,012
  • Last updated
    2023-11-08 v1
  • Checksum
    C8496D591EB49FD2
MKTAGNLVVLGSINADHILNLNSFPTPGETVTGSHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGESVRKQLAKDNIDIAPISVISGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQHERIAQASALLMQLESPIESVLAAAKIAHQNKTLVALNPAPARELSDELLALVDIITPNETEAEKLTGIRVENDKDAAKAAQALHAKGIHTVLITLGSRGVWASVNGEGQRVPGFKVDAVDTIAAGDTFNGALITALLEETPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIEAFLSQQR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAABKH010000003
EMBL· GenBank· DDBJ
MBW5272257.1
EMBL· GenBank· DDBJ
Genomic DNA

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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