ID IXTPA_ANADE Reviewed; 235 AA. AC Q2IEX2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 101. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=Adeh_3360; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., RA Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside CC triphosphates to their monophosphate derivatives, with a high CC preference for the non-canonical purine nucleotides XTP (xanthosine CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to CC function as a house-cleaning enzyme that removes non-canonical purine CC nucleotides from the nucleotide pool, thus preventing their CC incorporation into DNA/RNA and avoiding chromosomal lesions. CC {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: CC Reaction=XTP + H2O = XMP + diphosphate + H(+); Xref=Rhea:RHEA:28610, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; 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=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ITP + H2O = IMP + diphosphate + H(+); Xref=Rhea:RHEA:29399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. 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; CP000251; ABC83127.1; -; Genomic_DNA. DR RefSeq; WP_011422409.1; NC_007760.1. DR AlphaFoldDB; Q2IEX2; -. DR SMR; Q2IEX2; -. DR STRING; 290397.Adeh_3360; -. DR KEGG; ade:Adeh_3360; -. DR eggNOG; COG0127; Bacteria. DR HOGENOM; CLU_082080_0_2_7; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 1. DR FunFam; 3.90.950.10:FF:000001; dITP/XTP pyrophosphatase; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR020922; dITP/XTP_pyrophosphatase. 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; 2. DR SUPFAM; SSF52972; ITPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT CHAIN 1..235 FT /note="dITP/XTP pyrophosphatase" FT /id="PRO_1000068407" FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 7..12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 71 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 180..183 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 211 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 216..217 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" SQ SEQUENCE 235 AA; 24465 MW; BDF0A6FB224A2B89 CRC64; MDLLFGSTNP GKLRELRRLV AGLPLRVVSP DDLGRPLPVV VEDGATFQAN AEKKAVAWAR WSGLHAVADD SGLCVDALGG APGVHSARWS DLEPEGPASP VCELAGVAEL ELGPVAGRAA RDERNNDKLL AALSGLPDPR RGARYEAVLA LARPDGTLVG TVTGTCPGRI GHARRGDGGF GYDPLFVPAA ELAAGEGARV RTMAELSSDE KDALSHRGEA FRKLLPMLAA LARGA //