A0A7J8HH20 · A0A7J8HH20_MOLMO
- ProteinInosine triphosphate pyrophosphatase
- GeneITPA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids167 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Pyrophosphatase that hydrolyzes the non-canonical purine (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and 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
- ITP + H2O = IMP + diphosphate + 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 | 14-19 | ITP (UniProtKB | ChEBI) | ||||
Sequence: TGNAKK | ||||||
Binding site | 31 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 31-32 | ITP (UniProtKB | ChEBI) | ||||
Sequence: DT | ||||||
Binding site | 108-111 | ITP (UniProtKB | ChEBI) | ||||
Sequence: FGWD | ||||||
Binding site | 131 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 136-137 | ITP (UniProtKB | ChEBI) | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Molossidae > Molossus
Accessions
- Primary accessionA0A7J8HH20
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length167
- Mass (Da)18,280
- Last updated2021-04-07 v1
- Checksum3B85A360D8A436D2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7J8HGK1 | A0A7J8HGK1_MOLMO | ITPA | 208 | ||
A0A7J8HGL5 | A0A7J8HGL5_MOLMO | HJG59_006991 | 134 | ||
A0A7J8HHM3 | A0A7J8HHM3_MOLMO | HJG59_006991 | 148 |
Keywords
- Technical term