A0A2G5ZAW5 · A0A2G5ZAW5_9BACL

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 site9-11substrate
Binding site37-41substrate
Binding site136substrate
Binding site180ATP (UniProtKB | ChEBI)
Binding site206-211ATP (UniProtKB | ChEBI)
Binding site232K+ (UniProtKB | ChEBI)
Binding site234K+ (UniProtKB | ChEBI)
Binding site237-238ATP (UniProtKB | ChEBI)
Active site238Proton acceptor
Binding site238substrate
Binding site262ATP (UniProtKB | ChEBI)
Binding site268K+ (UniProtKB | ChEBI)
Binding site271K+ (UniProtKB | ChEBI)
Binding site273K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      CSV68_16300

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • P29
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina

Accessions

  • Primary accession
    A0A2G5ZAW5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-280Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    292
  • Mass (Da)
    31,018
  • Last updated
    2018-01-31 v1
  • Checksum
    2FF9D1761FB6FA97
MITVIGSANMDIIAQADKFPLQGETVRGKDFQTAPGGKGANQAVACARLGQNVQLIGTIGADSFGEMIVANLRNQQVDTTYITQAEAPSGVAIVLLTEGDNRIISIPGANHALTPQRIGELKSVIGASQLVMMQLELPIDTVWSVLKLCKELEVPVMMDPAPSSSFQLEYMPYVHYLTPNETESAQLFGTSIEETVSNYPIQLLVTLGKDGVCYHDREQIIYVPGVPAQVVDTTGAGDTFNGALASQLVQGNDLHSAVQFANVAASLSVGKFGAQGGMPTAQEVRNVTDKKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDYX01000042
EMBL· GenBank· DDBJ
PIC97836.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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