A1R3U8 · A1R3U8_PAEAT

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 site23-25substrate
Binding site51-55substrate
Binding site146substrate
Binding site187ATP (UniProtKB | ChEBI)
Binding site206-211ATP (UniProtKB | ChEBI)
Binding site234K+ (UniProtKB | ChEBI)
Binding site236K+ (UniProtKB | ChEBI)
Binding site239-240ATP (UniProtKB | ChEBI)
Active site240Proton acceptor
Binding site240substrate
Binding site264ATP (UniProtKB | ChEBI)
Binding site270K+ (UniProtKB | ChEBI)
Binding site273K+ (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
    • Ordered locus names
      AAur_1121

Organism names

Accessions

  • Primary accession
    A1R3U8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain16-278Carbohydrate kinase PfkB
Region32-51Disordered

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    302
  • Mass (Da)
    30,554
  • Last updated
    2007-02-06 v1
  • Checksum
    6F25345B472D8372
MSTSLQPSAPISSLTLTVMGSINLDITATANRLPSPGETVGGGVLRQQPGGKGANQAVAAARLAGSSRMVGAVGHDEAGQNLLSAMAAAGVDVHDVSRADAATGTALVLVDGEGENQIVVCPGANGAVNVDGVTFDDDEAVLCQLEVDQHVVLEAARRAKGFFALNAAPAMSLIPELLDRCDLVIVNETEYELIPALRHAPLVAVTYGGEGSAIFVDGERVAEAPAVRVTEIANTIGAGDAFCAALVLALRSGLEYSHALAAANAVGADAVRDASSQPALKPLEHYIEATRSSLAAGSAATK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000474
EMBL· GenBank· DDBJ
ABM08246.1
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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