E9AD19 · RBSK_LEIMA

  • Protein
    Ribokinase
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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. Specifically phosphorylates D-ribose. Fails to phosphorylate 4, 5 or 6 D-carbon sugars (erythrose, threose, xylulose, arabinose, fructose and glucose).

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.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.2 mMATP
0.3 mMribose
kcat is 10.2 sec-1 with ATP as substrate and 10.8 sec-1 with ribose as substrate.

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 site25-27substrate
Binding site53-57substrate
Binding site160substrate
Binding site209ATP (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 site302ATP (UniProtKB | ChEBI)
Binding site308K+ (UniProtKB | ChEBI)
Binding site311K+ (UniProtKB | ChEBI)
Binding site313K+ (UniProtKB | ChEBI)
Binding site317K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentglycosome
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process
Biological ProcessD-ribose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • ORF names
      LMJF_27_0420

Organism names

  • Taxonomic identifier
  • Strain
    • MHOM/IL/81/Friedlin
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    E9AD19

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004360261-329Ribokinase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    329
  • Mass (Da)
    35,342
  • Last updated
    2011-04-05 v1
  • Checksum
    FAD47833EFCEFE8E
MHRVQNVQSHVGEYAPDILVVGSCFLDYVGYVDHMPQVGETMHSESFHKGFGGKGANQAVAAGRLGAKVAMVSMVGTDGDGSDYIKELERNGVHTAYMLRTGKSSTGLAMILVDTKSSNNEIVICPNATNYFTPELLRAQTSNYEKILHTGLKYLICQNEIPLPTTLDTIKEAHSRGVYTVFNSAPAPKPAEVEQIKPFLPYVSLFCPNEVEAALITGMKVTDTESAFRAIKALQQLGVRDVVITLGAAGFALSENGAEPVHVTGKHVKAVDTTGAGDCFVGSMVYFMSRGRNLLEACKRANECAAISVTRKGTQLSYPHPSELPAGVT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR796423
EMBL· GenBank· DDBJ
CBZ12102.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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