H9L428 · H9L428_SALTY

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 site106-108substrate
Binding site134-138substrate
Binding site236substrate
Binding site280ATP (UniProtKB | ChEBI)
Binding site316-321ATP (UniProtKB | ChEBI)
Binding site342K+ (UniProtKB | ChEBI)
Binding site344K+ (UniProtKB | ChEBI)
Binding site347-348ATP (UniProtKB | ChEBI)
Active site348Proton acceptor
Binding site348substrate
Binding site378K+ (UniProtKB | ChEBI)
Binding site381K+ (UniProtKB | ChEBI)
Binding site383K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular FunctionDNA-binding transcription factor activity
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
      orf408
    • Synonyms
      rbsK
    • Ordered locus names
      STM1382

Organism names

Accessions

  • Primary accession
    H9L428

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Miscellaneous

PTM/Processing

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-58HTH deoR-type

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    408
  • Mass (Da)
    44,266
  • Last updated
    2012-05-16 v1
  • Checksum
    23455105EA2051A3
MFKEERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILNRDALSKLITENKIDISSTIATPIHQDAKLRRENPKKAGKVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSYSAYQTDKAPTGSALIYVSAVDGDNIIAIYPGANMMLTTQEINEQHRYIAESDVMLMQLETNIEALTEFIRLGKQENKMIMLNPAPYTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLICEHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGASSMPQHLQVLHRMRTQSNKVIHIN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE006468
EMBL· GenBank· DDBJ
AAL20306.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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