A0A2P6ML88 · A0A2P6ML88_ALKUR

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site247K+ (UniProtKB | ChEBI)
Binding site249K+ (UniProtKB | ChEBI)
Binding site252-253ATP (UniProtKB | ChEBI)
Active site253Proton acceptor
Binding site253substrate
Binding site277ATP (UniProtKB | ChEBI)
Binding site283K+ (UniProtKB | ChEBI)
Binding site286K+ (UniProtKB | ChEBI)
Binding site288K+ (UniProtKB | ChEBI)
Binding site292K+ (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
    • ORF names
      C6I21_00285

Organism names

Accessions

  • Primary accession
    A0A2P6ML88

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-292Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    305
  • Mass (Da)
    31,945
  • Last updated
    2018-05-23 v1
  • Checksum
    7F27DC9736F4FBAE
MARITVIGSYVTDLTGRTEKLPRPGETVIGRSFTMGPGGKGGNQAVAAARLGSDVTMVTKIGKDVFGEEAVRNFQAEKIRSEYVAVTPDAATGAAIIAVDDQGENMIVVTLGACGTLSADEVQQADAAIASSDYVLVQLETSIEAVEEAVRLAGEHRKPVILNPAPYHPVPEAVWQKVAYATPNETEAEGMTGVTVTDKETADHAARRIQQMGVENVIITLGKKGCYLLEQGQEGRLIPGIEVDAVDTTGAGDAFNGALAHYLGTEPSVEEACYKANVAAALSVTRAGTAPSMARAEEVASWSNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PVNS01000001
EMBL· GenBank· DDBJ
PRO67039.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp