C1AVJ2 · C1AVJ2_RHOOB

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.

Type
IDPosition(s)Description
Binding site13-15substrate
Binding site41-45substrate
Binding site140substrate
Binding site184ATP (UniProtKB | ChEBI)
Binding site205-210ATP (UniProtKB | ChEBI)
Binding site232K+ (UniProtKB | ChEBI)
Binding site234K+ (UniProtKB | ChEBI)
Binding site237-238ATP (UniProtKB | ChEBI)
Active site238Proton acceptor
Binding site238substrate
Binding site266K+ (UniProtKB | ChEBI)
Binding site269K+ (UniProtKB | ChEBI)
Binding site271K+ (UniProtKB | ChEBI)
Binding site275K+ (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
      ROP_10250

Organism names

  • Taxonomic identifier
  • Strain
    • B4
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus

Accessions

  • Primary accession
    C1AVJ2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-278Carbohydrate kinase PfkB

Sequence similarities

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
    288
  • Mass (Da)
    28,220
  • Last updated
    2009-05-26 v1
  • MD5 Checksum
    EB72E616B962A4DCED5C336B2943D49B
MSAPRVAVVGSVNMDLLTATERLPGPGETILGSAFAATPGGKGANQAIAAARAGGAVTFIGAVGSDVFALDLRQALVDAEVDTRYLREVDGPSGIAAITVDAAGENSIVVVPGANSTVADLTPAELAAVADADVLLCQLEIPLGTVVAAATHAAAHGTVVMVNPSPAQTLPPELVELIDVLLVNQTEAAQLGAEVTGAVSHVVTTLGSSGADYAGRDGAALHADSPVVEVVDTTGAGDAFAGALSVSWRGGPETAVPFACTAGALATTRRGASTSSPTLAEIEAALAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP011115
EMBL· GenBank· DDBJ
BAH49272.1
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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