A0A6A0H5W7 · A0A6A0H5W7_HYAAZ

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 site12-14substrate
Binding site22-26substrate
Binding site193substrate
Binding site238ATP (UniProtKB | ChEBI)
Binding site290-295ATP (UniProtKB | ChEBI)
Binding site322K+ (UniProtKB | ChEBI)
Binding site324K+ (UniProtKB | ChEBI)
Binding site327-328ATP (UniProtKB | ChEBI)
Active site328Proton acceptor
Binding site328substrate
Binding site360K+ (UniProtKB | ChEBI)
Binding site363K+ (UniProtKB | ChEBI)
Binding site365K+ (UniProtKB | ChEBI)
Binding site369K+ (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
      HAZT_HAZT006317

Organism names

  • Taxonomic identifier
  • Strain
    • HAZT.00-mixed
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Multicrustacea > Malacostraca > Eumalacostraca > Peracarida > Amphipoda > Senticaudata > Talitrida > Talitroidea > Hyalellidae > Hyalella

Accessions

  • Primary accession
    A0A6A0H5W7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-95Carbohydrate kinase PfkB
Domain147-372Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    383
  • Mass (Da)
    40,770
  • Last updated
    2020-06-17 v1
  • Checksum
    35FDD73519A3EE63
MLVDIVVVGSLVTDYITIGFGGKGANQCLMAAKLGAATAFVGKGMTMEMMMMGLGHDAVGDNYLDELKRTTINIDHVTRTSLAQSAVANVVVDDNGCGLVSRGWWYLLYGRLLGRKMLFHHIYEVALDARPKFVDRLRGLPAQVAAKLHCLGPDGGENCIVNIPGSNRLMTVEDVNAAAEVIKSAKVLICQNEISFDATKAALTIARQNGVVTVLNAGPAVPNLDPEILNNSDIVCVNETEKQYFPSLVLMYFWPSQAEVLTGVPVSGVADAVSAAKVLLTQGCREAVITLGAKGAVSLDLTSLAAGTDHEWVPAEKVVAVDTTGAGDAFIGAMAFYLAKMPTLPTKEKLRRSCAIATQSVLKPGAWLSLPAREELPSHLFDE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQDR03006106
EMBL· GenBank· DDBJ
KAA0200725.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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