A0A9P3KYA9 · A0A9P3KYA9_9VIRI

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 site22-24substrate
Binding site50-54substrate
Binding site289substrate
Binding site334ATP (UniProtKB | ChEBI)
Binding site370-375ATP (UniProtKB | ChEBI)
Binding site423K+ (UniProtKB | ChEBI)
Binding site425K+ (UniProtKB | ChEBI)
Binding site428-429ATP (UniProtKB | ChEBI)
Active site429Proton acceptor
Binding site429substrate
Binding site459K+ (UniProtKB | ChEBI)
Binding site462K+ (UniProtKB | ChEBI)
Binding site464K+ (UniProtKB | ChEBI)
Binding site468K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
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

    • ORF names
      CLOP_g9611

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NIES-67
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Zygnemophyceae > Zygnematophycidae > Desmidiales > Closteriaceae > Closterium > Closterium peracerosum-strigosum-littorale complex

Accessions

  • Primary accession
    A0A9P3KYA9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain15-127Carbohydrate kinase PfkB
Coiled coil120-147
Domain228-471Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    486
  • Mass (Da)
    47,487
  • Last updated
    2023-09-13 v1
  • Checksum
    F2668A5B9186DD3A
MASARTAQLAAGKALVVVGSANADVYVEVARMPLPGETVSATSGRTLPGGKGANQAAAAARLGHSTYLVGQVGSDANGAMLSAALSATGVHVDHLAVLGVPPGAAMSAGHPSVVAATNAKADAEAALEQAHAAAQRAQQAAATASKEAQAAGAGNFRTGAAAAAAATAQAEAEAAAAAQRAAAAAARAAAQAAAAADGQSAAAARQAASAAAAAGSVAGGGGEGSVATGHAIVMLQADGSNAIIIVGGANMAWSKRRMEGRGAGRRESYFSEGAREAIRGAGMVLLQRELPDDVNAEAAEVAAAAGVAVVLDMGGMEGALPDAMVRRVAVLSPNETELSRLTNLPVTSLPEAERAAHSLLAKGVPKVLVKLGSSGSLLVSSSPLAPPSSSSPLSASLSTATDGTGRQVWHLRQPVVPAHAVVDTTGAGDTFTAAYAVALLSGSSDADALLFASCAASLCVQKKGAMPSLPDRFSVQSLVQQSQNSW

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A9P3KXW2A0A9P3KXW2_9VIRICLOP_g9611541
A0A9P3KX35A0A9P3KX35_9VIRICLOP_g9611436

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BQMB01001722
EMBL· GenBank· DDBJ
GJP79371.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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