A0A4V0Z1J8 · A0A4V0Z1J8_9MICO

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 site12-14substrate
Binding site40-44substrate
Binding site140substrate
Binding site184ATP (UniProtKB | ChEBI)
Binding site225-230ATP (UniProtKB | ChEBI)
Binding site253K+ (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
    • ORF names
      EVS81_07305

Organism names

  • Taxonomic identifier
  • Strain
    • JW-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Leucobacter

Accessions

  • Primary accession
    A0A4V0Z1J8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-298Carbohydrate 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
    323
  • Mass (Da)
    32,298
  • Last updated
    2019-07-31 v1
  • Checksum
    062635869C20FDE9
MSRDVVVVGSANVDLVVEVPRRPGGGETLLGGDLQRLPGGKGANQAAAAARCGADAGIVACVGHDADGAFLRDRLSAAGVDTSTMIGVDGATGTAIIFLTPDGENSIVVSPGANAALDIERAEQHAAAWTGSRVLVLSLEIPAATAFRVAARAAACGTRVVLNAAPATRIAPETLRLCDPLIVNEHEARAALGDDTTDAAGLAVEDYERLAGRLREAGACSVVITLGPAGAVVAGGGAETPTRVAAHRVPVIDTTGAGDAFVGAVACELARGVDLVEAVRFATAVSAVSVQRVGAQASYADRAEVEAFIAARAETPGATATPR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP035806
EMBL· GenBank· DDBJ
QBE48659.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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