ID ITPA_DICDI Reviewed; 194 AA. AC Q54LQ6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 03-MAY-2023, entry version 106. 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 Name=itpa; ORFNames=DDB_G0286495; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-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 -!- 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; AAFI02000086; EAL64198.1; -; Genomic_DNA. DR RefSeq; XP_637700.1; XM_632608.1. DR AlphaFoldDB; Q54LQ6; -. DR SMR; Q54LQ6; -. DR STRING; 44689.DDB0238062; -. DR PaxDb; Q54LQ6; -. DR EnsemblProtists; EAL64198; EAL64198; DDB_G0286495. DR GeneID; 8625642; -. DR KEGG; ddi:DDB_G0286495; -. DR dictyBase; DDB_G0286495; itpa. DR eggNOG; KOG3222; Eukaryota. DR HOGENOM; CLU_082080_1_1_1; -. DR InParanoid; Q54LQ6; -. DR OMA; YDPIFQP; -. DR PhylomeDB; Q54LQ6; -. DR Reactome; R-DDI-74259; Purine catabolism. DR Reactome; R-DDI-9755088; Ribavirin ADME. DR PRO; PR:Q54LQ6; -. DR Proteomes; UP000002195; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0047429; F:nucleoside triphosphate diphosphatase activity; ISS:dictyBase. 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; ISS:dictyBase. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IBA:GO_Central. 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; IPR002637; Ham1p-like. DR InterPro; IPR027502; ITPase. DR InterPro; IPR029001; ITPase-like_fam. 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; Reference proteome. FT CHAIN 1..194 FT /note="Inosine triphosphate pyrophosphatase" FT /id="PRO_0000328399" FT BINDING 11..16 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 51 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 67..68 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 84 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 143..146 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 166 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" FT BINDING 171..172 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148" SQ SEQUENCE 194 AA; 21730 MW; B8A4AB1217C26D0E CRC64; MSISKKIVFV TGNAKKLEEA LQILGTSFPI ESKKVDLPEL QGDPIDISIE KCKIAAREVG GPVLVEDTCL CFNALKGLPG PYVKWFLDKL EPEGLYKLLD AWEDKSAYAL CNFAFSEGPD SEPIVFAGKT DGIIVQPRGP RNFGWDPVFQ PDGYKETYAE MDKSIKNTIS HRTRSLQKVK EFLKSKGYEN CKFE //