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 16-SEP-2015, entry version 74. 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=3.6.1.19 {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 (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; 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., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA 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., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA 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 CC distinguish between the deoxy- and ribose forms. Probably excludes CC non-canonical purines from RNA and DNA precursor pools, thus CC preventing their incorporation into RNA and DNA and avoiding CC chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {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 CC Mg(2+) 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 STRING; 44689.DDB0238062; -. DR EnsemblProtists; DDB0238062; DDB0238062; DDB_G0286495. DR EnsemblProtists; EAL64198; EAL64198; EBG00001265728. DR GeneID; 8625642; -. DR KEGG; ddi:DDB_G0286495; -. DR dictyBase; DDB_G0286495; itpa. DR eggNOG; COG0127; -. DR InParanoid; Q54LQ6; -. DR KO; K01519; -. DR OMA; GPYAEYV; -. DR PhylomeDB; Q54LQ6; -. DR PRO; PR:Q54LQ6; -. DR Proteomes; UP000002195; Chromosome 4. DR Proteomes; UP000002195; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0009204; P:deoxyribonucleoside triphosphate catabolic process; ISS:dictyBase. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. 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; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 194 Inosine triphosphate pyrophosphatase. FT /FTId=PRO_0000328399. FT REGION 11 16 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03148}. FT REGION 67 68 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03148}. FT REGION 143 146 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03148}. FT REGION 171 172 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03148}. FT METAL 39 39 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_03148}. FT METAL 67 67 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_03148}. FT BINDING 51 51 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03148}. FT BINDING 166 166 Substrate. {ECO:0000255|HAMAP- FT 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 //