A0A1L7NFA5 · A0A1L7NFA5_PSEPU

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 site12-14substrate
Binding site40-44substrate
Binding site141substrate
Binding site186ATP (UniProtKB | ChEBI)
Binding site222-227ATP (UniProtKB | ChEBI)
Binding site248K+ (UniProtKB | ChEBI)
Binding site250K+ (UniProtKB | ChEBI)
Binding site253-254ATP (UniProtKB | ChEBI)
Active site254Proton acceptor
Binding site254substrate
Binding site284K+ (UniProtKB | ChEBI)
Binding site287K+ (UniProtKB | ChEBI)
Binding site289K+ (UniProtKB | ChEBI)
Binding site293K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
    • ORF names
      KF715C_ch35860

Organism names

Accessions

  • Primary accession
    A0A1L7NFA5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-295Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    302
  • Mass (Da)
    30,933
  • Last updated
    2017-03-15 v1
  • Checksum
    C1825D96B37E5DE8
MNAKVVVVGSLNMDLVARAQRLPRAGETLPGDSFFTVPGGKGANQAVAVARLGGSVAMIGNVGDDDYGRQLHRALYVEGIDCQGVSTCPGVSSGVALITVDAASQNCIVIIPGGNGLLTPHSVQRFDALLQAAEVVICQLEVPADTVAWTLARARELGKQVILNPAPATGPLPAGWFACIDYLTPNESEAEALTGVAVTDQDSARRAGERLLQLGAGKVIITLGAQGALLVTAQGHQHYPAPVVQPLDTTAAGDTFIGGFAAGLVRGLEEGEAIAFGQRAAALSVTRAGAQPSIPYLAELTP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP015029
EMBL· GenBank· DDBJ
BAW24159.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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