A0A949K6S9 · A0A949K6S9_9FIRM

  • Protein
    Ribokinase
  • Gene
    rbsK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site11-13substrate
Binding site39-43substrate
Binding site140substrate
Binding site184ATP (UniProtKB | ChEBI)
Binding site220-225ATP (UniProtKB | ChEBI)
Binding site246K+ (UniProtKB | ChEBI)
Binding site248K+ (UniProtKB | ChEBI)
Binding site251-252ATP (UniProtKB | ChEBI)
Active site252Proton acceptor
Binding site252substrate
Binding site282K+ (UniProtKB | ChEBI)
Binding site285K+ (UniProtKB | ChEBI)
Binding site287K+ (UniProtKB | ChEBI)
Binding site291K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process
Biological Processlactose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • Name
      rbsK
    • ORF names
      KTH89_12155

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ASD5720
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Diplocloster

Accessions

  • Primary accession
    A0A949K6S9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain1-294Carbohydrate kinase PfkB
Coiled coil188-215

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. LacC subfamily.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    311
  • Mass (Da)
    33,386
  • Last updated
    2023-02-22 v1
  • Checksum
    B2D4E13512AC2B25
MGKVLVIGSINMDIVISVEHMPVGGENVYVNDVELICGGKGANQAGATAKLGLDTVYFGCVGQDENGKRLIDTLQQSGIDTSYMKVKDGGSGQCYIIVEGDGQNRILVSPGANEKMTVEDIDQVILPLIPELDMILTQLEIPLECVERIVQLGKEHGVKVFVDAGPIRGCKAEQLRGAWCISPNETELGALVERKVQTEEEIVKAAEELLALDVECVLVKLGGSGCLYISKDERIRQKSYKVNVVDTTAAGDSFSAGFAVGVLENKSTKDAIDYATKCGAIAVTKKGASPSLPTKEAVMNFEKEYLRNETL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHQCW010000018
EMBL· GenBank· DDBJ
MBU9737293.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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