A0A166HQF7 · A0A166HQF7_SECCO

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 site12-14substrate
Binding site40-44substrate
Binding site141substrate
Binding site186ATP (UniProtKB | ChEBI)
Binding site222-227ATP (UniProtKB | ChEBI)
Binding site249K+ (UniProtKB | ChEBI)
Binding site251K+ (UniProtKB | ChEBI)
Binding site254-255ATP (UniProtKB | ChEBI)
Active site255Proton acceptor
Binding site255substrate
Binding site280ATP (UniProtKB | ChEBI)
Binding site286K+ (UniProtKB | ChEBI)
Binding site289K+ (UniProtKB | ChEBI)
Binding site291K+ (UniProtKB | ChEBI)
Binding site295K+ (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
      TY91_01530

Organism names

Accessions

  • Primary accession
    A0A166HQF7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-298Carbohydrate 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
    310
  • Mass (Da)
    32,375
  • Last updated
    2016-07-06 v1
  • MD5 Checksum
    E4BC7F3213BCB9EE06F3ED02C99B37EB
MTNRVTVIGSLNVDTILEIPRLPKPGETLAMHNQSFAGGGKGSNQGIAAGRAGADTYFIGKIGDDTNGKFMINSMKESGINVDQVTITKDAKTGQAFILLDDKGQNSILVYGGANQKLAVDDVKNAENTIADSDFIITQFETPLDVAEAAFKTAKANDVVTILNPAPARQAIPASLLAVSDLVVPNETESQTLTGVEITDEASMVKAADKMHAMGAKCVIITVGSKGAFYHTADGNTGFVDAFKVKAVDTTAAGDTFIGALSSQLKKDMSNLPEAIRFANRASSITVQRMGAHPSIPTLAEIEAADAAAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JYDC01000015
EMBL· GenBank· DDBJ
KZL43019.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help