A0A8D5U088 · A0A8D5U088_9CREN

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.

Type
IDPosition(s)Description
Binding site9-11substrate
Binding site37-41substrate
Binding site132substrate
Binding site173ATP (UniProtKB | ChEBI)
Binding site204-209ATP (UniProtKB | ChEBI)
Binding site230K+ (UniProtKB | ChEBI)
Binding site232K+ (UniProtKB | ChEBI)
Binding site235-236ATP (UniProtKB | ChEBI)
Active site236Proton acceptor
Binding site236substrate
Binding site260ATP (UniProtKB | ChEBI)
Binding site266K+ (UniProtKB | ChEBI)
Binding site269K+ (UniProtKB | ChEBI)
Binding site271K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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

    • Name
      rbsK
    • ORF names
      HS7_01780

Organism names

Accessions

  • Primary accession
    A0A8D5U088

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-274Carbohydrate 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
    286
  • Mass (Da)
    30,971
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    CAE243E58C089EA3A713E6F3EE132E75
MITVVGSYNVDLIIRVEKFPQASETVFTEGVKVYHGGKGSNQAVSASRLNGRVTLIAAVGNDNYGEEAIKFWQEEKVDTSYVKVKRGRTGMAYILVNRKGENMIVVDRGANSMLTSSDLDGTLGKVTLIQLEVNMDVVKTALTKSHGVKILNPAPVVSEVRSLLEMVDVLTPNEIEFMELTGTNDLSYGTLVLLKRVNKAVIVTLGEKGAFLATRNRAFRIPSPKVKPVDTTGAGDVFNAALAVALHEEMDLEDAVSFANKVASVSVMTEGALGPTIEEVRKHFEV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP024596
EMBL· GenBank· DDBJ
BCU66741.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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