F2DXU4 · F2DXU4_HORVV

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 site58-60substrate
Binding site86-90substrate
Binding site190substrate
Binding site235ATP (UniProtKB | ChEBI)
Binding site271-276ATP (UniProtKB | ChEBI)
Binding site299K+ (UniProtKB | ChEBI)
Binding site301K+ (UniProtKB | ChEBI)
Binding site304-305ATP (UniProtKB | ChEBI)
Active site305Proton acceptor
Binding site305substrate
Binding site335K+ (UniProtKB | ChEBI)
Binding site338K+ (UniProtKB | ChEBI)
Binding site340K+ (UniProtKB | ChEBI)
Binding site344K+ (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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Hordeinae > Hordeum

Accessions

  • Primary accession
    F2DXU4

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain51-347Carbohydrate 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
    361
  • Mass (Da)
    37,083
  • Last updated
    2011-05-31 v1
  • Checksum
    E056E2BF1750E353
MALEARLRLPLAGPTPATAFVSGSNPKPSHVSFSLKPTSTSLAAANAPPPIVVVGSANADIYVEVNRLPLVGETVAASAGHSLAGGKGANQAACGGRLAMGPTYLVARVGDDANGRLLEGALADAGGVRLDRVARAPGAPSGHAVVMLMPDGQNSIIIVGGANMEGWAPEVDPEDLDLIRQAGVLLLQREIPDWVNIQVAQAAKGAGVPVILDAGGMDAPVPRELLELVDIFSPNETELARLTGMLTETFEQISQAAGACHKMGVKEVLVKLGSQGSALFVEGEEPIRQAIIPATEVVDTTGAGDTFTSAFAVALVEGKPKKECMRFAAAAASLCVRVKGAIPSMPDRETVMSLLEPVQAE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK368712
EMBL· GenBank· DDBJ
BAJ99915.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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