A0A0U3G9W5 · A0A0U3G9W5_9ACTN

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.

TypeIDPosition(s)Description
Binding site13-15substrate
Binding site41-45substrate
Binding site141substrate
Binding site184ATP (UniProtKB | ChEBI)
Binding site219-224ATP (UniProtKB | ChEBI)
Binding site245K+ (UniProtKB | ChEBI)
Binding site247K+ (UniProtKB | ChEBI)
Binding site250-251ATP (UniProtKB | ChEBI)
Active site251Proton acceptor
Binding site251substrate
Binding site281K+ (UniProtKB | ChEBI)
Binding site284K+ (UniProtKB | ChEBI)
Binding site286K+ (UniProtKB | ChEBI)
Binding site290K+ (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
      AS200_28635

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CdTB01
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A0U3G9W5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain5-293Carbohydrate kinase PfkB
Region302-321Disordered

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    321
  • Mass (Da)
    32,249
  • Last updated
    2016-03-16 v1
  • Checksum
    AA17959B9FD449E7
MYDYDLLVVGSANADLVIGVERRPEAGETVLGSDLAVHPGGKGANQAVAAARLGARTALLARVGDDAYGRLLLDSQRAAGVDTAGVLAGGAPTGVALITVDPSGDNSIVVSPGANGRLTPDDVRAAAGLLQRSRVVSAQLEIPLETVVEAVRSLAEGSRFVLNPSPPRPLPAEVLAACDPLIVNEHEAKVVLGEACASERPEDWARLLLAKGPRSVVITLGAQGALVASADGVERVPSTKVDAVDTTGAGDAFTAALAWRLGTGTGLAEAAAYAARVGAAAVTREGAQESFPTAEEVESLCCADPAGAPRTPGSGSAGESL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP013743
EMBL· GenBank· DDBJ
ALV35566.1
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.
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