A0A255G738 · A0A255G738_9ACTN
- ProteindITP/XTP pyrophosphatase
- GenerdgB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids209 (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
- H2O + ITP = diphosphate + H+ + IMP
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15-20 | substrate | ||||
Sequence: TNNAKK | ||||||
Active site | 77 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 77 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 78 | substrate | ||||
Sequence: S | ||||||
Binding site | 160-163 | substrate | ||||
Sequence: FGYD | ||||||
Binding site | 183 | substrate | ||||
Sequence: K | ||||||
Binding site | 188-189 | substrate | ||||
Sequence: HR |
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 > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Enemella
Accessions
- Primary accessionA0A255G738
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length209
- Mass (Da)22,040
- Last updated2017-12-20 v1
- ChecksumA681BC685A68C0C9
Keywords
- Technical term