A0A0G3UD93 · A0A0G3UD93_9ACTN

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 site19-21substrate
Binding site47-51substrate
Binding site146substrate
Binding site187ATP (UniProtKB | ChEBI)
Binding site231-236ATP (UniProtKB | ChEBI)
Binding site258K+ (UniProtKB | ChEBI)
Binding site260K+ (UniProtKB | ChEBI)
Binding site263-264ATP (UniProtKB | ChEBI)
Active site264Proton acceptor
Binding site264substrate
Binding site294K+ (UniProtKB | ChEBI)
Binding site297K+ (UniProtKB | ChEBI)
Binding site299K+ (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
    • ORF names
      M444_00855

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Mg1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A0G3UD93

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-300Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    323
  • Mass (Da)
    32,243
  • Last updated
    2015-09-16 v1
  • Checksum
    58972CBBD4CA7D60
MPEAVPGTSPQVVVIGSVNIDHVVVADAFPSPGETLLGRTAYVTLGGKGANQAAAAASGGVRTAMIARVGEDAEADRARARLVAGGVDVEAVTTVPGAETGTAWITTAAGDNTIVVVAGANHQWPSEGDPTEGLGAQAAVVLAQLEIPLDVVRRAADACRGRFLLNAAPAAELPDDLIARCDVLIVNEHEQAVVSGQLATDNDAEVTPDEASVRKAHDALRARGAKAVVTTLGEAGAIVTDADGVSTALPAVPTTVVDTTGAGDAFAGVLAARLAAGDSLLDAARLGIAAGSLAVRVSGAPQQYADLATLRALAPTTPPTEKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011664
EMBL· GenBank· DDBJ
AKL64234.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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