A0A7S4AXR9 · A0A7S4AXR9_9STRA
- ProteinMultifunctional fusion protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids607 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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.
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic activity
- D-ribose + ATP = D-ribose 5-phosphate + ADP + H+
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 82-84 | substrate | |||
Binding site | 110-114 | substrate | |||
Binding site | 217 | substrate | |||
Binding site | 267 | ATP (UniProtKB | ChEBI) | |||
Binding site | 306-311 | ATP (UniProtKB | ChEBI) | |||
Binding site | 344 | K+ (UniProtKB | ChEBI) | |||
Binding site | 346 | K+ (UniProtKB | ChEBI) | |||
Binding site | 349-350 | ATP (UniProtKB | ChEBI) | |||
Active site | 350 | Proton acceptor | |||
Binding site | 350 | substrate | |||
Binding site | 380 | K+ (UniProtKB | ChEBI) | |||
Binding site | 383 | K+ (UniProtKB | ChEBI) | |||
Binding site | 385 | K+ (UniProtKB | ChEBI) | |||
Binding site | 389 | K+ (UniProtKB | ChEBI) | |||
Binding site | 422-427 | ITP (UniProtKB | ChEBI) | |||
Binding site | 455 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 467 | ITP (UniProtKB | ChEBI) | |||
Binding site | 483 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 483-484 | ITP (UniProtKB | ChEBI) | |||
Binding site | 559-562 | ITP (UniProtKB | ChEBI) | |||
Binding site | 583 | ITP (UniProtKB | ChEBI) | |||
Binding site | 588-589 | ITP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside triphosphate diphosphatase activity | |
Molecular Function | ribokinase activity | |
Biological Process | D-ribose catabolic process | |
Biological Process | deoxyribonucleoside triphosphate catabolic process | |
Biological Process | nucleotide metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameInosine triphosphate pyrophosphatase
- EC number
- Short namesITPase ; Inosine triphosphatase
- Alternative names
- Recommended nameRibokinase
- EC number
- Short namesRK
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Stramenopiles > Ochrophyta > Bacillariophyta > Bacillariophyceae > Bacillariophycidae > Bacillariales > Bacillariaceae > Pseudo-nitzschia
Accessions
- Primary accessionA0A7S4AXR9
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-24 | ||||
Chain | PRO_5031394745 | 25-607 | Multifunctional fusion protein | ||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 73-391 | Carbohydrate kinase PfkB | |||
Sequence similarities
Belongs to the HAM1 NTPase family.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length607
- Mass (Da)65,651
- Last updated2021-06-02 v1
- MD5 Checksum4F64825368A546ADEFC89F7DAE82BB21
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HBIX01034442 EMBL· GenBank· DDBJ | CAE0729723.1 EMBL· GenBank· DDBJ | Transcribed RNA |