I1BT58 · I1BT58_RHIO9
- ProteinInosine triphosphate pyrophosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids697 (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
- 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 | 520-525 | ITP (UniProtKB | ChEBI) | |||
Binding site | 548 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 560 | ITP (UniProtKB | ChEBI) | |||
Binding site | 576 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 576-577 | ITP (UniProtKB | ChEBI) | |||
Binding site | 652-655 | ITP (UniProtKB | ChEBI) | |||
Binding site | 675 | ITP (UniProtKB | ChEBI) | |||
Binding site | 680-681 | ITP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | acetate-CoA ligase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | dITP diphosphatase activity | |
Molecular Function | ITP diphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | XTP diphosphatase activity | |
Biological Process | acetyl-CoA biosynthetic process from acetate | |
Biological Process | deoxyribonucleoside triphosphate catabolic 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 > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Rhizopodaceae > Rhizopus
Accessions
- Primary accessionI1BT58
Proteomes
Organism-specific databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-332 | AMP-dependent synthetase/ligase | |||
Domain | 393-471 | AMP-binding enzyme C-terminal | |||
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Belongs to the HAM1 NTPase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length697
- Mass (Da)77,041
- Last updated2012-06-13 v1
- MD5 Checksum8523188772D00790F7E84F14E9A0F948
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH476733 EMBL· GenBank· DDBJ | EIE79388.1 EMBL· GenBank· DDBJ | Genomic DNA |