A0A2S5X2B7 · A0A2S5X2B7_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.
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 site16-18substrate
Binding site44-48substrate
Binding site145substrate
Binding site189ATP (UniProtKB | ChEBI)
Binding site225-230ATP (UniProtKB | ChEBI)
Binding site251K+ (UniProtKB | ChEBI)
Binding site253K+ (UniProtKB | ChEBI)
Binding site256-257ATP (UniProtKB | ChEBI)
Active site257Proton acceptor
Binding site257substrate
Binding site287K+ (UniProtKB | ChEBI)
Binding site290K+ (UniProtKB | ChEBI)
Binding site292K+ (UniProtKB | ChEBI)
Binding site296K+ (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
      C5C17_15475

Organism names

  • Taxonomic identifier
  • Strain
    • RFBA6
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Pseudoclavibacter

Accessions

  • Primary accession
    A0A2S5X2B7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-299Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    309
  • Mass (Da)
    30,832
  • Last updated
    2018-07-18 v1
  • Checksum
    2547865C989CF449
MSGLERAGVLVVGSVSADLTAFSTRAPGHGETLRGESFSLALGGKGANQAVAAARAGAPTAFIGCVGEDAFGEMVVRELRSAGVAVGGVRAVARETGIAHIRVDATGENSIVIVPGANDALEESMVLQGIGDAAATSSVLLTQLETPERLTDCILRTARDAGLTTILDPAPAVALDGKVWASVDIVTPNETEARMLTGVVVESEASAAQAGRWFLDRGVGAALITRGGAGTTLVTTDHVETFPVVQVEVVDTTAAGDAFAGALGAALAGGQPLEAAIRYGAAAGALAVSRRGASPSIPTAAAIEALLAR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PSUA01000015
EMBL· GenBank· DDBJ
PPG38052.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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