Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

E3QA66 · E3QA66_COLGM

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.

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 site17-19substrate
Binding site45-49substrate
Binding site161substrate
Binding site205ATP (UniProtKB | ChEBI)
Binding site244-249ATP (UniProtKB | ChEBI)
Binding site271K+ (UniProtKB | ChEBI)
Binding site273K+ (UniProtKB | ChEBI)
Binding site276-277ATP (UniProtKB | ChEBI)
Active site277Proton acceptor
Binding site277substrate
Binding site307ATP (UniProtKB | ChEBI)
Binding site313K+ (UniProtKB | ChEBI)
Binding site316K+ (UniProtKB | ChEBI)
Binding site318K+ (UniProtKB | ChEBI)
Binding site322K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
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

    • ORF names
      GLRG_02898

Organism names

Accessions

  • Primary accession
    E3QA66

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-325Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    330
  • Mass (Da)
    34,538
  • Last updated
    2011-01-11 v1
  • MD5 Checksum
    AE9CDAA731B4634A50245C0C30E0C4D9
MMTASKTPQITVLGSLNIDLTSYVPHHPLPGETLTSNSVVISPGGKGANQAVACAKLSRSRDAPNDAANESASVSMIGAVGSDSYGDLLLKNLGEHGVHTDRIAVGNDLKTGMAIIVVDEPTGQNRIILAPEANHAVTPDKFGSLPETLTPKPDLLVMQLEVPLETVLAALRSAKAAAVPVLLNPAPAQRLPDEAYDGLAHLVVNETEAAILSGCHESELDTPEGLKRVGEWFMAKKVLNVIITLGGRGVYYINQDGAADLIPAQKVKVVDTTAAGDTFVGSYCVAAVNAQAKGEAFDISSAIKNANRAAAKTVERKGAQTSIPWRDELL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG697338
EMBL· GenBank· DDBJ
EFQ27754.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help