A0A261Y136 · A0A261Y136_9FUNG
- ProteinInosine triphosphate pyrophosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids926 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
- H2O + ITP = diphosphate + H+ + IMP
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 | 758-763 | ITP (UniProtKB | ChEBI) | ||||
Sequence: TGNKNK | ||||||
Binding site | 786 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 798 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 880-883 | ITP (UniProtKB | ChEBI) | ||||
Sequence: FGWD | ||||||
Binding site | 903 | ITP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 908-909 | ITP (UniProtKB | ChEBI) | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | cellulase activity | |
Molecular Function | cellulose binding | |
Molecular Function | dITP diphosphatase activity | |
Molecular Function | ITP diphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | monoatomic cation transmembrane transporter activity | |
Molecular Function | nucleotide binding | |
Molecular Function | XTP diphosphatase activity | |
Biological Process | cellulose catabolic process | |
Biological Process | deoxyribonucleoside triphosphate catabolic process | |
Biological Process | inorganic ion homeostasis | |
Biological Process | intracellular monoatomic cation homeostasis | |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Endogonomycetes > Endogonales > Endogonales incertae sedis > Bifiguratus
Accessions
- Primary accessionA0A261Y136
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MVKILLTVVALSIAAVHA | ||||||
Chain | PRO_5012311616 | 19-926 | Inosine triphosphate pyrophosphatase | |||
Sequence: DNLSPGGTATRYWDCCKPSGGISGKAAVNRPVFSCAQDGVTHVDPSTNSACAGGTAYTCTNYQPFVSSCNPNLSYAFGARAQSNDESTFECACYQVTFAQLPGKTLIVQATNDGGDVPATNFDIQIPGGGVGLFDACTAEYNAPPGGWGAQYGGISSQTQCSQLPASLQKGCNWRFTWFADNPTISSISRVKCPSQLTDLSGCIRNDDASQPAPSVGCNGPQPSTSNMSTSTSKASSTPKPTATCAALYAQCGGQGYTGPTCCISSTCQYQNPSEFADKDLVLDTFAFMLRFTSTLGHSTMFVCRRTCHPQSGLFQGSSGTISPRARLVTGGLFVRQGRFLSTLRPDNPQDKTSSTPSSHPDSHSHSHSHGHAHGHEGHSHAHLVDALETTSSRGWRITVVGLVANVGLCVTKGVAGWVMNSASLVADAAHSLSDMISDFVTLYTYRVSRRPPDELHPYGYGKYETVGSLAVSSILIVGALGIGYHSYELLLQVLPETFTGALNSNALPDAAVASAPTSHASVDAGIAAAKEAHEGASLSNLLPFHSHAHEHHDTLLNPNAAWFALASVIIKEWLYQATIKVGKDERSDVLIANAWHHRSDAFSSIVALAAIAGSHFGVPILDPLGGILVSGMILKTGVEIMLGSLKELVDANVDDDVLQQVQQAITRLQKTQPDLIDFHSIRGRKAGPFILVDLILQVNPTLTVEKAHRVEDAVRRARSNLRIDNYRESMGKHQLVFVTGNKNKLAEVQAILGDTVDLVNRSLDLPEIQGTPEEVARAKCIAAAEQDHVSPKIPVSALTLFKGYPVHTWHEGLNKLLAGYEDKSAYALCIFALSKGPGEVPILFEGRTDGRIVPARGPNNFGWDPIFEPTGFDETYAEMPKSTKNTISHRFRALEKLSAYLSHYPPQ |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 229-256 | Disordered | ||||
Sequence: QPAPSVGCNGPQPSTSNMSTSTSKASST | ||||||
Compositional bias | 230-256 | Polar residues | ||||
Sequence: PAPSVGCNGPQPSTSNMSTSTSKASST | ||||||
Domain | 262-299 | CBM1 | ||||
Sequence: TCAALYAQCGGQGYTGPTCCISSTCQYQNPSEFADKDL | ||||||
Compositional bias | 361-380 | Polar residues | ||||
Sequence: TLRPDNPQDKTSSTPSSHPD | ||||||
Region | 361-399 | Disordered | ||||
Sequence: TLRPDNPQDKTSSTPSSHPDSHSHSHSHGHAHGHEGHSH |
Sequence similarities
Belongs to the HAM1 NTPase family.
Belongs to the glycosyl hydrolase 45 (cellulase K) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length926
- Mass (Da)99,012
- Last updated2017-11-22 v1
- Checksum6DE1BBC6EF9E65DB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 230-256 | Polar residues | ||||
Sequence: PAPSVGCNGPQPSTSNMSTSTSKASST | ||||||
Compositional bias | 361-380 | Polar residues | ||||
Sequence: TLRPDNPQDKTSSTPSSHPD |
Keywords
- Technical term