A4I2M8 · A4I2M8_LEIIN

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 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 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
      LINJ_27_0430

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JPCM5
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    A4I2M8
  • Secondary accessions
    • A0A2K4YXD2
    • A0A381MKP3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-320Carbohydrate kinase PfkB

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)
    35,398
  • Last updated
    2007-05-01 v1
  • Checksum
    5F97E8013E6859A9
MHRARNVRSHTGEYAPDILVVGSCFLDYVGYVDHMPQVGETMHSVSFHKGFGGKGANQAVAAGRLGAKVAMVSMVGTDGDGSDYIKELERNGVDTAYMFRTGKSSTGLAMILVDTKSSNNEIVICPNATNHFTPELLRAQTNNYERILHTGLKYLICQNEIPLPTTLDTIKEAHSRGVYTVFNSAPAPKPAEVEQIKPFLPYVSLFCPNEVEATLITGVKVTDTESAFSAIKALQQLGVRDVVITLGAAGFVLSENGVEPVHVTGKHVKAVDTTGAGDCFVGSMVYFMSRGRNLLEACKRANECAAISVTRKGTQLSYPHPSELPAGVM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR796459
EMBL· GenBank· DDBJ
CAM69023.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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