A9T794 · A9T794_PHYPA

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 site14-16substrate
Binding site42-46substrate
Binding site148substrate
Binding site193ATP (UniProtKB | ChEBI)
Binding site229-234ATP (UniProtKB | ChEBI)
Binding site257K+ (UniProtKB | ChEBI)
Binding site259K+ (UniProtKB | ChEBI)
Binding site262-263ATP (UniProtKB | ChEBI)
Active site263Proton acceptor
Binding site263substrate
Binding site293K+ (UniProtKB | ChEBI)
Binding site296K+ (UniProtKB | ChEBI)
Binding site298K+ (UniProtKB | ChEBI)
Binding site302K+ (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • ORF names
      PHYPA_008890

Organism names

Accessions

  • Primary accession
    A9T794

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-305Carbohydrate 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
    320
  • Mass (Da)
    33,255
  • Last updated
    2008-02-05 v1
  • MD5 Checksum
    841079B7C0BB426FAD3F98C639226CEA
MTIGSPLVVVGSVNADIYVEVERLPAEGETIAARSGQTLPGGKGANQAACAARLSYPTFFCGQVGQDAHANLVRNALVSAGVHLDHVNTVDAPTGHAVVILQPGGKNSIIIVGGANVAWPKLEDGISSLTTNAQELIKRAGAVLLQREIPDAVNLEAAKIAKSAGVPVIMDAGGAEGPIPEELLKCLTVLSPNETELARLTDMPTNSGEEILTAAKKVLEMGVKQVLVKMGENGSMLVSEKESPIHQPAILAPVVVDTTGAGDTFTAAYAVALIERQTLVEALRFAAASASICVRFKGAMPSMPERKAVLQLLKEHPVSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ABEU02000006
EMBL· GenBank· DDBJ
PNR52516.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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