ID ITPA_ENCCU Reviewed; 192 AA. AC Q8SS24; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE Short=ITPase {ECO:0000255|HAMAP-Rule:MF_03148}; DE Short=Inosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_03148}; GN OrderedLocusNames=ECU04_1180; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as inosine triphosphate (ITP), deoxyinosine CC triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their CC respective monophosphate derivatives. The enzyme does not distinguish CC between the deoxy- and ribose forms. Probably excludes non-canonical CC purines from RNA and DNA precursor pools, thus preventing their CC incorporation into RNA and DNA and avoiding chromosomal lesions. CC {ECO:0000255|HAMAP-Rule:MF_03148}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+); CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03148}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03148}; CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) CC or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03148}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}. CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03148}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_03148}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL590444; CAD25306.1; -; Genomic_DNA. DR RefSeq; NP_584802.1; NM_001041152.1. DR AlphaFoldDB; Q8SS24; -. DR SMR; Q8SS24; -. DR STRING; 284813.Q8SS24; -. DR GeneID; 858950; -. DR KEGG; ecu:ECU04_1180; -. DR VEuPathDB; MicrosporidiaDB:ECU04_1180; -. DR HOGENOM; CLU_082080_1_0_1; -. DR InParanoid; Q8SS24; -. DR OMA; QWDCVFI; -. DR OrthoDB; 479at2759; -. DR Proteomes; UP000000819; Chromosome IV. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:RHEA. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:RHEA. DR GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR CDD; cd00515; HAM1; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_03148; HAM1_NTPase; 1. DR InterPro; IPR027502; ITPase. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR002637; RdgB/HAM1. DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1. DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; ITPase-like; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..192 FT /note="Inosine triphosphate pyrophosphatase" FT /id="PRO_0000413139" FT BINDING 8..13 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 46 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 64..65 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 81 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 141..144 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 164 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 169..170 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" SQ SEQUENCE 192 AA; 21149 MW; F6BA42A8B3B40F82 CRC64; MGRIYFATTN LKKLKEIRSL FEADIVHMNI PMVEIQASLE RIVDHKLNQV VPCIGEGDAV IVDDTAVAFE GLYGFPGVYI KDFLRIGSRK ISEIVGKIGN SNATAFCCLG IAHYRDGRVV KKVFFGELEG SIVESKEDGL EGFDYIFLPS GSSMCLGDMP VDEKNRISHR RIASKKLADY MASVGIIKAH GS //