A0A1B8GJ44 · A0A1B8GJ44_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.

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 site161substrate
Binding site205ATP (UniProtKB | ChEBI)
Binding site245-250ATP (UniProtKB | ChEBI)
Binding site272K+ (UniProtKB | ChEBI)
Binding site274K+ (UniProtKB | ChEBI)
Binding site277-278ATP (UniProtKB | ChEBI)
Active site278Proton acceptor
Binding site278substrate
Binding site314K+ (UniProtKB | ChEBI)
Binding site317K+ (UniProtKB | ChEBI)
Binding site319K+ (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
      VE01_06113

Organism names

  • Taxonomic identifier
  • Strain
    • UAMH 10579
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Pseudeurotiaceae > Pseudogymnoascus

Accessions

  • Primary accession
    A0A1B8GJ44

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain7-325Carbohydrate kinase PfkB
Compositional bias26-40Polar residues
Region26-67Disordered
Compositional bias50-67Polar residues

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    333
  • Mass (Da)
    34,952
  • Last updated
    2016-11-02 v1
  • Checksum
    9EB5703AE5A9A203
MAPQRVITVIGSINADLVTVTDRVPQGGETLTSKSFGTGAGGKGANQGVAAARTSRSNPKNSSSAEALQSDVDVRFIGAVGSDPFGPSITAGMKADGLDVTRIKVVEGQSTGVAVILVEEATGENRILFNPGANYTLRPEQFTNIKDLGTPKPDLVILQLEIPLDTVLTIIELCKAANVAVLLNPAPAVPLPDTVFVGLEHLVVNETEAAIISGRSVDSVNAENFDWDVVTDDFLNKGVKNVVVTLGGKGSYSSSAIGKGSLLRANKVKVVDTTCAGDTFVGAYGSLYVKALEKEGSWDLKEAVRKSSKASELTVQRQGAQEAIPWSDEINWD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias26-40Polar residues
Compositional bias50-67Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV460232
EMBL· GenBank· DDBJ
OBT95851.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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