A0A226BXV1 · A0A226BXV1_9FIRM

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.
Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site10-12substrate
Binding site38-42substrate
Binding site139substrate
Binding site183ATP (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 Componentcytosol
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Molecular Functiontagatose-6-phosphate kinase activity
Biological ProcessD-ribose catabolic process
Biological ProcessD-tagatose 6-phosphate catabolic process
Biological Processlactose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • Name
      rbsK
    • ORF names
      CDO51_10725

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 18760
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Natranaerobiales > Natranaerobiaceae > Natranaerobius

Accessions

  • Primary accession
    A0A226BXV1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-293Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. LacC subfamily.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    306
  • Mass (Da)
    32,802
  • Last updated
    2017-10-25 v1
  • Checksum
    951488C2E83E36CC
MKLSVLGSLNMDFVYYVSRLPKEGETLLAEDNAKFPGGKGANQAVAAARLGSDVKMIGAVGDDDLGDSLLESLQKESIDISGVKQMTDINTGNAFITVDSKGNNTILVYSGANSKVDLKWVDNFKKDIRESDFLLTQLETPLDIVTKGIELAFDVGTKVVLNPAPGLTLPNELLEKVYLLTPNQTELSIISGREIKTDDDLITASRSLIDLGVQNVVVTLGSKGALHIDKTSYTFIESFNVNAIDTTAAGDSFTAGLTFGIWRGKSIKEALQYASAVSALTVIKEGAQSSLPTANQVEMYLEKGEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NIQC01000029
EMBL· GenBank· DDBJ
OWZ83029.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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