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A0A2W1B4G1 · A0A2W1B4G1_UNCCH

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 site5-7substrate
Binding site33-37substrate
Binding site134substrate
Binding site178ATP (UniProtKB | ChEBI)
Binding site214-219ATP (UniProtKB | ChEBI)
Binding site240K+ (UniProtKB | ChEBI)
Binding site242K+ (UniProtKB | ChEBI)
Binding site245-246ATP (UniProtKB | ChEBI)
Active site246Proton acceptor
Binding site246substrate
Binding site276K+ (UniProtKB | ChEBI)
Binding site279K+ (UniProtKB | ChEBI)
Binding site281K+ (UniProtKB | ChEBI)
Binding site285K+ (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
      DK304_001349

Organism names

Accessions

  • Primary accession
    A0A2W1B4G1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain2-288Carbohydrate kinase PfkB
Region282-301Disordered

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
    301
  • Mass (Da)
    31,533
  • Last updated
    2018-09-12 v1
  • MD5 Checksum
    9D4F3E00DB6E33231B2A8524B196196B
MGSLNFDLIATVPRFPNPGESLIGREFYTSSGGKGGNQAVAASRLGAEAFMVGRVGDDNFGAEMLESLHVYGVNTSGVTVEPGFQSGIAHITIDESGENKIVIVPGANSSCDESEIEQVNLRLRFADVLLLQLELPLELSMKAANQAKNLGKIVVFDPAPAKALPLSTYGNIDYLIPNETEASVLAGFPVEDPINAVDAAVLLRSQGVDTVIIKMGDQGVSYATDGDKGHLPGFSVKAVDTVAAGDAFNGAFSVAIAEGKSLRNAITWGMAAGALAVTKRGAHSSMPSRNDVERLILEQSR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QGNO01000020
EMBL· GenBank· DDBJ
PZC49348.1
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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