A0A263HAU7 · A0A263HAU7_9PAST
- ProteindITP/XTP pyrophosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids198 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic activity
- ITP + H2O = IMP + diphosphate + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 9-14 | substrate | |||
Binding site | 41 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 70 | Proton acceptor | |||
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 71 | substrate | |||
Binding site | 157-160 | substrate | |||
Binding site | 180 | substrate | |||
Binding site | 185-186 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | dITP diphosphatase activity | |
Molecular Function | ITP diphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | XTP diphosphatase activity | |
Biological Process | nucleotide metabolic process | |
Biological Process | purine nucleoside triphosphate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namedITP/XTP pyrophosphatase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Actinobacillus
Accessions
- Primary accessionA0A263HAU7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)21,102
- Last updated2017-12-20 v1
- Checksum270E3A202576ED76
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
UFSB01000001 EMBL· GenBank· DDBJ | SUU37622.1 EMBL· GenBank· DDBJ | Genomic DNA |