A0AAC9IG92 · A0AAC9IG92_9BACI

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 site11-13substrate
Binding site39-43substrate
Binding site139substrate
Binding site183ATP (UniProtKB | ChEBI)
Binding site210-215ATP (UniProtKB | ChEBI)
Binding site236K+ (UniProtKB | ChEBI)
Binding site238K+ (UniProtKB | ChEBI)
Binding site241-242ATP (UniProtKB | ChEBI)
Active site242Proton acceptor
Binding site242substrate
Binding site266ATP (UniProtKB | ChEBI)
Binding site272K+ (UniProtKB | ChEBI)
Binding site275K+ (UniProtKB | ChEBI)
Binding site277K+ (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
      BK049_10555

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • VV3
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0AAC9IG92

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-284Carbohydrate kinase PfkB

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
    292
  • Mass (Da)
    30,892
  • Last updated
    2024-05-29 v1
  • Checksum
    13FF2700E1E4B307
MSQIVVVGSCSMDLVVTSNKRPNAGETVLGESFKTVPGGKGANQAVASARLGADVYMVGRVGDDAYGQDIIRNLQAQGVRTTYMKPVTDMESGTAHIILAEGDNSIVVVKGANNEVTPHYVNEALSSIEDIGMVLIQQEIPEETVEAVCAICSEKGIPVILNPAPARQVSQQIFNQAAYITPNEHEAALMFDGLTIAEALRQYPNKLLITEGKNGVRYFDGSKEVLVPGYPVKAVDTTGAGDTFNGALAVALIEGKSLYDALAFANLAASISVTKFGAQGGMPTRDELEKKE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017786
EMBL· GenBank· DDBJ
AOZ89085.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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