A0A8X7TDX4 · A0A8X7TDX4_CANPA

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.

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 site13-15substrate
Binding site41-45substrate
Binding site144substrate
Binding site190ATP (UniProtKB | ChEBI)
Binding site231-236ATP (UniProtKB | ChEBI)
Binding site259K+ (UniProtKB | ChEBI)
Binding site261K+ (UniProtKB | ChEBI)
Binding site264-265ATP (UniProtKB | ChEBI)
Active site265Proton acceptor
Binding site265substrate
Binding site295K+ (UniProtKB | ChEBI)
Binding site298K+ (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI)
Binding site304K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
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
      RBK1
    • ORF names
      FOB60_000133

Organism names

  • Taxonomic identifier
  • Strain
    • FDAARGOS_652
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    A0A8X7TDX4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-306Carbohydrate kinase PfkB

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    311
  • Mass (Da)
    33,272
  • Last updated
    2022-12-14 v1
  • Checksum
    F3548CDE1723B0E7
MQKPTITVIGSLNYDLVTFTNKVPEGGETYQANSFETHMGGKGLNEAIAVARLSPEGKVNTRMVGRVGTDQFGDSLKQCLVDAGVDVSNVKAIDGSSGVAVIIVEENGENRILITPGANGKLSLSDEEYASIFKYDAFVVLQNEYPDTAKSITWLKTHKPEINIAYNPSPYKPKLITHEILSKIDLLIVNEGEAKDVAKHLLGGSTAQFDTLAVELQKLLHQGNIKTVVITMGSKGSIFYNGEADPTFVPSKKIQSVVDTTGAGDTFFGAVVSNLALGNNLEQAVNFATTASSLAIQKKGAAESIPFYKDV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABWAB010000001
EMBL· GenBank· DDBJ
KAF6058551.1
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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