AC MF_03148; DC Protein; auto TR HAMAP; MF_03148; -; 1; level=0 XX Names: HAM1_NTPase XX ID ITPA DE RecName: Full=Inosine triphosphate pyrophosphatase; DE Short=ITPase; DE Short=Inosine triphosphatase; DE EC=3.6.1.9; DE AltName: Full=Non-canonical purine NTP pyrophosphatase; DE AltName: Full=Non-standard purine NTP pyrophosphatase; DE AltName: Full=Nucleoside-triphosphate diphosphatase; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase; DE Short=NTPase; case GN Name=ITPA; else case GN Name=hap-1; else case GN Name=HAM1; end case XX case CC -!- FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine CC (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate CC (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective CC monophosphate derivatives. The enzyme does not distinguish between the CC deoxy- and ribose forms. Probably excludes non-canonical purines from CC RNA and DNA precursor pools, thus preventing their incorporation into CC RNA and DNA and avoiding chromosomal lesions. else case CC -!- FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine CC (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate CC (dHAPTP) and 5-bromodeoxyuridine 5'-triphosphate (BrdUTP) to their CC respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) CC is also a potential substrate. The enzyme does not distinguish between CC the deoxy- and ribose forms. Probably excludes non-canonical purines CC from RNA and DNA precursor pools, thus preventing their incorporation CC into RNA and DNA and avoiding chromosomal lesions. else 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. end case 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) CC or Mn(2+).; CC -!- SUBUNIT: Homodimer. case CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. else CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. XX DR Pfam; PF01725; Ham1p_like; 1; trigger=no DR NCBIfam; TIGR00042; TIGR00042; 1; trigger=no XX case KW Acetylation end case case KW Nucleus end case KW Cytoplasm KW Hydrolase KW Magnesium KW Manganese KW Metal-binding KW Nucleotide metabolism KW Nucleotide-binding XX case GO GO:0005634; C:nucleus end case GO GO:0005737; C:cytoplasm GO GO:0047429; F:nucleoside triphosphate diphosphatase activity GO GO:0009204; P:deoxyribonucleoside triphosphate catabolic process XX FT From: ITPA_HUMAN (Q9BY32) case FT INIT_MET Nter FT /note="Removed" FT Group: 1; Condition: M FT MOD_RES Nter+1 FT /note="N-acetylalanine" FT Group: 1; Condition: A end case FT BINDING 14..19 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: T-x-N-x-x-K FT BINDING 72..73 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: D-[TS] FT BINDING 149..152 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: F-G-W-[DEN] FT BINDING 177..178 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: H-R FT BINDING 44 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 72 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 56 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: K FT BINDING 172 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT Condition: [KR] XX Size: 183-234; Related: None; Template: Q9BY32; Q9D892; P47119; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in TRYCR Plasmid: None Comments: None XX # Revision 1.14 2023/06/01 //