A0A154P6D5 · A0A154P6D5_DUFNO

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 site12-14substrate
Binding site40-44substrate
Binding site141substrate
Binding site185ATP (UniProtKB | ChEBI)
Binding site221-226ATP (UniProtKB | ChEBI)
Binding site242ATP (UniProtKB | ChEBI)
Binding site249K+ (UniProtKB | ChEBI)
Binding site251K+ (UniProtKB | ChEBI)
Binding site254-255ATP (UniProtKB | ChEBI)
Active site255Proton acceptor
Binding site255substrate
Binding site287K+ (UniProtKB | ChEBI)
Binding site290K+ (UniProtKB | ChEBI)
Binding site292K+ (UniProtKB | ChEBI)
Binding site296K+ (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
      WN55_09393

Organism names

  • Taxonomic identifier
  • Strain
    • 0120121106
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Apoidea > Anthophila > Halictidae > Rophitinae > Dufourea

Accessions

  • Primary accession
    A0A154P6D5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-299Carbohydrate 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
    309
  • Mass (Da)
    33,002
  • Last updated
    2016-06-08 v1
  • Checksum
    7E346693EF1605E2
MSPKIVVVGSCMIDFTSYSPRLPKSGETLVGSNFEIKYGGKGANQCVAAAKLGASTAIVASLGSDVYAQEYLKIFKKENVNVAHVQIQENQHSGIAHITVADNGENHIVIVSGSNESLSLKHVDAAAEVVRDAAVLLCQFETPLETTRHALKLHKDHGLSIVNGAPAMEHVDYDLLSLCDIFCVNETEAEIMTGVQPLGLSNMQEAIDKLLDNGCNTVILTLGKMGAAYASRKNRTATLVPTRRVKPVDTTGAGDAFLGAIAYFKAYHPGLSMDECIRRACVVATESVLKLGTHASFPTRSSLSPDLFV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ434826
EMBL· GenBank· DDBJ
KZC07401.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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