A0A922I5E5 · A0A922I5E5_DERFA

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 site18-20substrate
Binding site46-50substrate
Binding site148substrate
Binding site195ATP (UniProtKB | ChEBI)
Binding site231-236ATP (UniProtKB | ChEBI)
Binding site258K+ (UniProtKB | ChEBI)
Binding site260K+ (UniProtKB | ChEBI)
Binding site263-264ATP (UniProtKB | ChEBI)
Active site264Proton acceptor
Binding site264substrate
Binding site290ATP (UniProtKB | ChEBI)
Binding site296K+ (UniProtKB | ChEBI)
Binding site299K+ (UniProtKB | ChEBI)
Binding site301K+ (UniProtKB | ChEBI)
Binding site305K+ (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
      DERF_005207
      , HUG17_3734

Organism names

  • Taxonomic identifier
  • Strains
    • Derf
    • JKM2019
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Analgoidea > Pyroglyphidae > Dermatophagoidinae > Dermatophagoides

Accessions

  • Primary accession
    A0A922I5E5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-308Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    318
  • Mass (Da)
    35,027
  • Last updated
    2023-02-22 v1
  • Checksum
    A356B3F82F940706
MEIDDNHPRVCSFMGASVMDLISYVDRFPEPGETMVGNNFRKGFGGKAANACIMAARLGLECRMLAKIGNDTFGDEMIENFQQHNISTEFVLKCPDVMTGTAAIIVTRKGDNNIVYVPGATNSLTPEEINKLSDSLFKDCRLFVSTFECTPESLHAALLLARKHKVPTLINGAPPFPKPMENSHIYPLCDILCVNESEAKLMTKLRVDTIDDCRIACKMILDKGCGSVILTMGANGALYVNRHQALHIPVPNKIQPLDTTGAGDSFMGSLAFYLVHFPNLTIEETIKRCNIIASTAVTRPGTQDSYPHRNELPEELFL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SDOV01000007
EMBL· GenBank· DDBJ
KAH7639701.1
EMBL· GenBank· DDBJ
Genomic DNA
ASGP02000002
EMBL· GenBank· DDBJ
KAH9521563.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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