A0A3P9BSM0 · A0A3P9BSM0_9CICH

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.

Type
IDPosition(s)Description
Binding site15-17substrate
Binding site43-47substrate
Binding site144substrate
Binding site189ATP (UniProtKB | ChEBI)
Binding site225-230ATP (UniProtKB | ChEBI)
Binding site253K+ (UniProtKB | ChEBI)
Binding site255K+ (UniProtKB | ChEBI)
Binding site258-259ATP (UniProtKB | ChEBI)
Active site259Proton acceptor
Binding site259substrate
Binding site285ATP (UniProtKB | ChEBI)
Binding site291K+ (UniProtKB | ChEBI)
Binding site294K+ (UniProtKB | ChEBI)
Binding site296K+ (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process
Biological Processnucleoside phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • Name
      RBKS

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Cichlomorphae > Cichliformes > Cichlidae > African cichlids > Pseudocrenilabrinae > Haplochromini > Maylandia > Maylandia zebra complex

Accessions

  • Primary accession
    A0A3P9BSM0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-302Carbohydrate 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
    314
  • Mass (Da)
    33,546
  • Last updated
    2019-02-13 v1
  • MD5 Checksum
    9D33D52B6B4093B0250C0B6AA843181D
MTEKVFDIVVVGSCMTDLVSKAPRLPKAGETIHGHKFFIGFGGKGANQCIQAARLGVKTAMVCKVGKDFFGDNYIQNFKDNGVHTEFVKQSSDAVTGAASITVDDAGENAIVIVAGANMLLGAEELQEALPAISHTKVLVCQLEISPQTSLQAMCMARDNKVKTIFNPAPAIPDLDPDFYRVSDVFCCNESEAELLTGTSVASVEEAHRAGQKLLKRGCGSVIVTLGPQGCVVLKGGEPTLKHVPAPEVTAVDTTGAGDSFIGALAFYMANHPHMPLEEMARRANLVAGVSVREIGTQTSFPYRRDLPNEYFQE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3P9BRR3A0A3P9BRR3_9CICHRBKS297

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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