A0A7W5IMI9 · A0A7W5IMI9_9BURK

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site11-13substrate
Binding site39-43substrate
Binding site138substrate
Binding site182ATP (UniProtKB | ChEBI)
Binding site211-216ATP (UniProtKB | ChEBI)
Binding site238K+ (UniProtKB | ChEBI)
Binding site240K+ (UniProtKB | ChEBI)
Binding site243-244ATP (UniProtKB | ChEBI)
Active site244Proton acceptor
Binding site244substrate
Binding site266ATP (UniProtKB | ChEBI)
Binding site272K+ (UniProtKB | ChEBI)
Binding site275K+ (UniProtKB | ChEBI)
Binding site277K+ (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
      FHW21_005657

Organism names

  • Taxonomic identifier
  • Strain
    • WP4_3_2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A7W5IMI9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-284Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    296
  • Mass (Da)
    30,985
  • Last updated
    2021-06-02 v1
  • Checksum
    999D41021A221267
MARVVVVGSINMDMVVTTDTFPRLGETLFGTRFSTFPGGKGANQAVAAARLGAQVTMIGCVGADAFGEQMKQTLAREGIDVSHIRTGQESTGIASITLSGADNAIIVVPGANNELSPEDIDRASDAFAQADVILAQLETPMDTVLHAARRAREHAKPFFLNPAPAVALSDELVSLTTLLTPNEHELATALQTPSGWWAEVLSRMPGRIAMTHGKEGAYFTHADGTLVHQPGFAVEAVDTTGAGDTFNGAMAAFWHLGMAEAVRRANAAGALSVTRAGAQGGMPTLAELEQFLSQQS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHYP010000020
EMBL· GenBank· DDBJ
MBB3260786.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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