B2JR99 · B2JR99_PARP8

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 site17-19substrate
Binding site45-49substrate
Binding site146substrate
Binding site190ATP (UniProtKB | ChEBI)
Binding site226-231ATP (UniProtKB | ChEBI)
Binding site255K+ (UniProtKB | ChEBI)
Binding site258-259ATP (UniProtKB | ChEBI)
Active site259Proton acceptor
Binding site259substrate
Binding site289K+ (UniProtKB | ChEBI)
Binding site292K+ (UniProtKB | ChEBI)
Binding site294K+ (UniProtKB | ChEBI)
Binding site298K+ (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
      Bphy_4655

Organism names

Accessions

  • Primary accession
    B2JR99

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-300Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    319
  • Mass (Da)
    32,579
  • Last updated
    2008-06-10 v1
  • Checksum
    2D5C5D972F2EA9A7
MAVQQKEGRVVILGIYVTDLTFRADRMPLIGETVAGNAFKMGPGGKGSNQAVAAARAGADVVFVTRIGNDAFGAIARSTWDAEGITARASVVDGASTGAAHIFVDDMTGKNAIIVASGAAGLMNAGDVDAIEADIASARVFVTQLEQPVCAARRGLEVARKHGVTTVFNPAPALPLDDSIFPLCDYITPNETETAALTGIEVRNVDDARRAADVLLNKGVRNVIVTLGEAGALLHSAEQSVFVPAFQCGRVVETAGAGDGFTGGFAAALARGADAVEALRFGCALAGISVTRPGTAPSMPMLAEVNAVLAQAGHPLSTH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001044
EMBL· GenBank· DDBJ
ACC73765.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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