E3KAB5 · ITPA_PUCGT
- ProteinInosine triphosphate pyrophosphatase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids192 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
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
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H+This reaction proceeds in the forward direction.
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 | 10-15 | ITP (UniProtKB | ChEBI) | ||||
Sequence: TGNANK | ||||||
Binding site | 46 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 58 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 74-75 | ITP (UniProtKB | ChEBI) | ||||
Sequence: DT | ||||||
Binding site | 91 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 149-152 | ITP (UniProtKB | ChEBI) | ||||
Sequence: FGWD | ||||||
Binding site | 172 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 177-178 | ITP (UniProtKB | ChEBI) | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | dITP diphosphatase activity | |
Molecular Function | ITP diphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside triphosphate diphosphatase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | XTP diphosphatase activity | |
Biological Process | deoxyribonucleoside triphosphate catabolic process | |
Biological Process | nucleoside 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 > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Pucciniomycetes > Pucciniales > Pucciniaceae > Puccinia
Accessions
- Primary accessionE3KAB5
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000413148 | 1-192 | Inosine triphosphate pyrophosphatase | |||
Sequence: MGALKLVFVTGNANKLREVKKILSTDVSSEDSLKIEVDSKALDLPEVQGSTQDVAREKSRAAAKLIGGPCITEDTALCFKAMGGLPGPYIKWFLEKLGLDGLNKMLQGFSSTEATALCTFAYCEPGKEPILFEGATEGNIVPARGPTNFGWDPIFEVSGTGMTYAEMPAEQKNSLSHRSKALDKLRQHFSRR |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length192
- Mass (Da)20,845
- Last updated2011-01-11 v1
- Checksum55506B5295813B3B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS178278 EMBL· GenBank· DDBJ | EFP81272.1 EMBL· GenBank· DDBJ | Genomic DNA |