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A0A2A2ZWY3 · A0A2A2ZWY3_MYCAV

  • Protein
    Ribokinase
  • Gene
    rbsK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Type
IDPosition(s)Description
Binding site11-13substrate
Binding site39-43substrate
Binding site138substrate
Binding site185ATP (UniProtKB | ChEBI)
Binding site202-207ATP (UniProtKB | ChEBI)
Binding site228K+ (UniProtKB | ChEBI)
Binding site230K+ (UniProtKB | ChEBI)
Binding site233-234ATP (UniProtKB | ChEBI)
Active site234Proton acceptor
Binding site234substrate
Binding site268K+ (UniProtKB | ChEBI)
Binding site271K+ (UniProtKB | ChEBI)
Binding site273K+ (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
      CKJ66_15025

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FLAC0165
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)

Accessions

  • Primary accession
    A0A2A2ZWY3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    292
  • Mass (Da)
    29,360
  • Last updated
    2017-12-20 v1
  • MD5 Checksum
    B87BA7CF44B60FFABD560F7C6A59640D
MTDVCVVGSVNLDLSLAVDALPRPGETVLASSLRQAPGGKGGNQAVAAARAGARVQFVGAVGDDAAAGQLRAHLQANGVGLDGAVEIPGPSGTAIVVVDANAENTIVVAPGANGRFTLNDERARAVLAGCDVMLTQLEIPVATAVAAARHARSGGAVVVVNASPAGRDPDSLSELAAAADVVITNEEEASEWPWRPRHLVVTLGSHGARYVGADGEYSVPSPDVDAVDTTGAGDVFAGVLAANWPLEPGSPDQRRLALRRACAAGALATLVPGAGDCAPRAEEIERALRGKS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NSFD01000039
EMBL· GenBank· DDBJ
PBA25957.1
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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