A0A0F4YRR6 · A0A0F4YRR6_TALEM

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 site162substrate
Binding site222ATP (UniProtKB | ChEBI)
Binding site267-272ATP (UniProtKB | ChEBI)
Binding site306K+ (UniProtKB | ChEBI)
Binding site308K+ (UniProtKB | ChEBI)
Binding site311-312ATP (UniProtKB | ChEBI)
Active site312Proton acceptor
Binding site312substrate
Binding site366K+ (UniProtKB | ChEBI)
Binding site369K+ (UniProtKB | ChEBI)
Binding site371K+ (UniProtKB | ChEBI)
Binding site375K+ (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
      T310_5442

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 393.64
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Rasamsonia

Accessions

  • Primary accession
    A0A0F4YRR6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-134Carbohydrate kinase PfkB
Domain207-378Carbohydrate 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
    382
  • Mass (Da)
    40,593
  • Last updated
    2015-06-24 v1
  • Checksum
    98C5DD3CC8A2AC88
MAPLIRVIGSLNVDMVSVTPRFPGPGETITATSFMTSAGGKGANQAVACGRLSRSRPSSTSSSSSASPVKVEMVGAVGGRDGHFQTLLRPTLESSGLDTSRIRTIEDAYTGVAVIVVDSSAGGENRIFFSPGANYSGMQPIPEVLGTGLAAPVPDIIVMQGEIPVDTVIGILREIRAFKEKNRRDGKKGIEAGPEVIFNPAPAPPGGLPEDVYATVDHLIMNESEAELMTPKTEQLLRVVPEAAGESDREKVARYFHKLGVTYVVITLGAKGVWYSATDAGTSGPADGVTRFVNEIPAAKVEKVLDTTAAGDTFVGGYAVHIARWREHRRAQGKSGQDLAGDDKKERYQNIIDEAMKRATRAAARCVERAGAMDSIPWEDEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LASV01000251
EMBL· GenBank· DDBJ
KKA20546.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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