A0A177ZIK3 · A0A177ZIK3_9BACI

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 site12-14substrate
Binding site40-44substrate
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)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Molecular Functiontagatose-6-phosphate kinase activity
Biological ProcessD-ribose catabolic process
Biological ProcessD-tagatose 6-phosphate 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
      ABB05_21770

Organism names

Accessions

  • Primary accession
    A0A177ZIK3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-294Carbohydrate kinase PfkB

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    304
  • Mass (Da)
    32,099
  • Last updated
    2016-09-07 v1
  • Checksum
    134C4C23B59EA1DA
MAYDIAVVGSINMDVIVDTPNYPEYGDTLFCDSIAMKPGGKGANQAVSVAKLGKKSCLIGAVGNDSAGKQLIQNLNSKNVDTTHILQSEESGTGTFVAMIDSTGENTMVGTKGANDSLTSEDITKTFAQIDAKILLIQMETSRESIIAAMKAAKERNMYVVLDPAPADGIFDEAFKYADLITPNKQETKRITGIEVTDEASALEAAKKLNELGIKDVIVKMGEDGSLIYQNGQATIVDAIKVKAVDTVGAGDCFAGALASSYLDTNDLIESAKFASVAAGIKVSRHGGQEAIPTLKEVESYLIK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LDJR01000061
EMBL· GenBank· DDBJ
OAK67180.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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