A0A9W7C6N6 · A0A9W7C6N6_9STRA
- ProteinInosine triphosphate pyrophosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids595 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine.
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
- (5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine + GDP + H+
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 413-418 | ITP (UniProtKB | ChEBI) | ||||
Sequence: TGNKKK | ||||||
Binding site | 440 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 452 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 468 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 468-469 | ITP (UniProtKB | ChEBI) | ||||
Sequence: DT | ||||||
Binding site | 544-547 | ITP (UniProtKB | ChEBI) | ||||
Sequence: FGWD | ||||||
Binding site | 572 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 577-578 | ITP (UniProtKB | ChEBI) | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | amino acid kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside triphosphate diphosphatase activity | |
Molecular Function | nucleotide binding | |
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 nameInosine triphosphate pyrophosphatase
- EC number
- Short namesITPase ; Inosine triphosphatase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Stramenopiles > Ochrophyta > Bolidophyceae > Parmales > Triparmaceae > Triparma
Accessions
- Primary accessionA0A9W7C6N6
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 53-274 | Aminoglycoside phosphotransferase | ||||
Sequence: YDDENFLLSHTTSTNITTKYLVKVHNGVESESASIIDYQNKIMLHLNGADGITTTTPLTCDSGDLCVTTPLPVQSPSHSPSPLCVRLLTYIEGTPMAYKNVTADLLHDAGEYLANVDSSLDNFDHPAAKRFHAWDQRNTTSLREFVQYIQTQERQAMISDIIDVFEKTVLVDDEKLRKGVLQSDFNDANIILDGSDKLAGVIDFGDSVYSWRVLDLSVAMAY |
Sequence similarities
Belongs to the HAM1 NTPase family.
Belongs to the aminoglycoside phosphotransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length595
- Mass (Da)65,475
- Last updated2023-11-08 v1
- ChecksumEBFE05AF3B599609
Keywords
- Technical term