A0A2N3NB25 · A0A2N3NB25_9PEZI

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 site14-16substrate
Binding site42-46substrate
Binding site153substrate
Binding site197ATP (UniProtKB | ChEBI)
Binding site236-241ATP (UniProtKB | ChEBI)
Binding site263K+ (UniProtKB | ChEBI)
Binding site265K+ (UniProtKB | ChEBI)
Binding site268-269ATP (UniProtKB | ChEBI)
Active site269Proton acceptor
Binding site269substrate
Binding site294ATP (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI)
Binding site303K+ (UniProtKB | ChEBI)
Binding site305K+ (UniProtKB | ChEBI)
Binding site309K+ (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

    • ORF names
      jhhlp_004265

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JHH-5317
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Microascales > Microascaceae > Lomentospora

Accessions

  • Primary accession
    A0A2N3NB25

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-312Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    316
  • Mass (Da)
    33,359
  • Last updated
    2018-04-25 v1
  • Checksum
    991464C25E2E471D
MAPKPIVAVIGSLNVDVVTYVTRVPQGGETIAANGFHIGLGGKGANQAVACAKVSRSQDDIQNGTAIVKMIGAVGDDSYGPLVVDGLKGVGIDTSDIQTRTGHKTGVSTIIVEEATGENRILFSAHANATVRPDEYATDLPRPLPDLIIMQLEIPLETVTQILTTAQRVGVPVLFNPAPAQRIDTKYYPGITHLVVNETEAAILSGREVKELETEDGQARIAEIFHGWGSKYVLITLGGNGVYYSVAGGARGHVDAEKVKAVDTTAAGDTFVGVYALEVVKADFDVEKAVCRANLAASKTVTRKGAQESIPWLDEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NLAX01000010
EMBL· GenBank· DDBJ
PKS09646.1
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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