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A0A5J5DW93 · A0A5J5DW93_9BIFI

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 site39-41substrate
Binding site67-71substrate
Binding site167substrate
Binding site214ATP (UniProtKB | ChEBI)
Binding site255-260ATP (UniProtKB | ChEBI)
Binding site283K+ (UniProtKB | ChEBI)
Binding site285K+ (UniProtKB | ChEBI)
Binding site288-289ATP (UniProtKB | ChEBI)
Active site289Proton acceptor
Binding site289substrate
Binding site319K+ (UniProtKB | ChEBI)
Binding site322K+ (UniProtKB | ChEBI)
Binding site324K+ (UniProtKB | ChEBI)
Binding site328K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
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
      EM848_08110

Organism names

  • Taxonomic identifier
  • Strain
    • RST8
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A5J5DW93

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain32-328Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    34,743
  • Last updated
    2019-12-11 v1
  • MD5 Checksum
    FF11BBB39D88608FF95BB33D0F636067
MPANAPELIALLDRLTAATPADAAAGKPSAPVAVIGSMNADYTVVTERLPRPGETVTAGPLRVLPGGKSGNQAASAARLGADVRMFGAVGSDANADFLLGELGKAGVDTCNVLRAQGASGTTVITVDAHGENTIVYSPGSNALVSADYVVSRRDALTGARVLGLCLESPIDTVTAAARLCHDAGVTVLLNNSPFVPAHDLPADLVAATDILLVNEHEMAMMLDVEEPANGRWIAFDWQEALAGMAALGFPRAIVTLGAEGSVVLDADSGVASHVDPVAVDAVDTTGCGDAFMGTVLAGLAAEFDLRDAVRLASAVSAYAATGQGAQASYGSADRIRDWLVAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RZOA01000015
EMBL· GenBank· DDBJ
KAA8822805.1
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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