Q5E4V3 · Q5E4V3_ALIF1

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 site11-13substrate
Binding site39-43substrate
Binding site140substrate
Binding site184ATP (UniProtKB | ChEBI)
Binding site220-225ATP (UniProtKB | ChEBI)
Binding site246K+ (UniProtKB | ChEBI)
Binding site248K+ (UniProtKB | ChEBI)
Binding site251-252ATP (UniProtKB | ChEBI)
Active site252Proton acceptor
Binding site252substrate
Binding site276ATP (UniProtKB | ChEBI)
Binding site282K+ (UniProtKB | ChEBI)
Binding site285K+ (UniProtKB | ChEBI)
Binding site287K+ (UniProtKB | ChEBI)
Binding site291K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
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
    • Ordered locus names
      VF_1448

Organism names

Accessions

  • Primary accession
    Q5E4V3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-294Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    305
  • Mass (Da)
    31,838
  • Last updated
    2005-03-15 v1
  • Checksum
    CE734F7A999EBD0F
MNKLVVLGSVNADHVLQVASFPRPGETLHGHSYSVIPGGKGANQAVAAARLGADIAFIASVGDDSFGHQMIEAFQFDGINTEAVMIEENTPTGIAMIQVAATGENSICISAEANARLTADRIAPHHGLIEAADTLLMQLETPIETIEKAAQIAKAAGTKVVLNPAPAHQLSDDLLQLVDIITPNETEAELLTGIQVTDMASAQQAADALHAKGIETVMITLGSKGVWISQNGSGRQVEGFKVQATDTTGAGDTFNGAFLTGLQSGRKLDDAIKFAHAAAAISVTRMGAQTSIPSITEVERFLLEH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000020
EMBL· GenBank· DDBJ
AAW85943.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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