A0A016C3P8 · A0A016C3P8_BACFG
- ProteindITP/XTP pyrophosphatase
- GenerdgB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids194 (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 | |||
Active site | 70 | Proton acceptor | |||
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 71 | substrate | |||
Binding site | 151-154 | substrate | |||
Binding site | 174 | substrate | |||
Binding site | 179-180 | 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 > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A016C3P8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length194
- Mass (Da)21,620
- Last updated2014-06-11 v1
- MD5 Checksum63DFF46B7CEE9F634D8D1310D58CEC35
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JGDS01000028 EMBL· GenBank· DDBJ | EXZ75527.1 EMBL· GenBank· DDBJ | Genomic DNA |