A0A0G9F715 · A0A0G9F715_LACPN

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 site11-13substrate
Binding site39-43substrate
Binding site140substrate
Binding site185ATP (UniProtKB | ChEBI)
Binding site221-226ATP (UniProtKB | ChEBI)
Binding site247K+ (UniProtKB | ChEBI)
Binding site249K+ (UniProtKB | ChEBI)
Binding site252-253ATP (UniProtKB | ChEBI)
Active site253Proton acceptor
Binding site253substrate
Binding site278ATP (UniProtKB | ChEBI)
Binding site284K+ (UniProtKB | ChEBI)
Binding site287K+ (UniProtKB | ChEBI)
Binding site289K+ (UniProtKB | ChEBI)
Binding site293K+ (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
      AYO51_13995
      , JH395_05700
      , Lp19_2006
      , LPJSA22_02091
      , NAB2_0525

Organism names

Accessions

  • Primary accession
    A0A0G9F715

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-296Carbohydrate 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
    306
  • Mass (Da)
    31,769
  • Last updated
    2015-09-16 v1
  • Checksum
    439D9E8C20C0289D
MNKVTVLGSLNVDSILRFKRFPKPGETLPLTGKSVAGGGKGANQAIAAARAGAQTTFIGKVGTDQEGAFMVQQLTNSGVNDQYVQHSNVASTGSAFILLDSSSENRILIDGGTNQQVTAEDVERAQPAISASTFLIAQFETPIAATIRGFELAQAAGQKTILNPAPATTTVPAELLATTDLIVPNETETETLTGVHITDEQSMIQGAQKLQALGVANVIITVGSKGAFWMRGAEHGFVPAYKVEAVDTTAAGDTFIGALSSVLMPDFSNLAAAVRFANRASSIAVQKLGAQPSIPTKEAIEAAERA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LSST01000031
EMBL· GenBank· DDBJ
KYK53098.1
EMBL· GenBank· DDBJ
Genomic DNA
LUXM01000033
EMBL· GenBank· DDBJ
KZU94032.1
EMBL· GenBank· DDBJ
Genomic DNA
LUXO01000011
EMBL· GenBank· DDBJ
KZV05879.1
EMBL· GenBank· DDBJ
Genomic DNA
MCOL01000001
EMBL· GenBank· DDBJ
ODO62086.1
EMBL· GenBank· DDBJ
Genomic DNA
CP066817
EMBL· GenBank· DDBJ
QQM62048.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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