ID A0A0L8HK24_OCTBM Unreviewed; 189 AA. AC A0A0L8HK24; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 02-OCT-2024, entry version 34. DE RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148}; GN ORFNames=OCBIM_22012863mg {ECO:0000313|EMBL:KOF89577.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89577.1}; RN [1] {ECO:0000313|EMBL:KOF89577.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF89577.1}; RC TISSUE=Gonad {ECO:0000313|EMBL:KOF89577.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03148}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148}; CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) CC or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_03148, CC ECO:0000256|RuleBase:RU003781}. 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; KQ417945; KOF89577.1; -; Genomic_DNA. DR RefSeq; XP_014771708.1; XM_014916222.1. DR AlphaFoldDB; A0A0L8HK24; -. DR EnsemblMetazoa; XM_014916222.2; XP_014771708.1; LOC106870217. DR EnsemblMetazoa; XM_052967189.1; XP_052823149.1; LOC106870217. DR GeneID; 106870217; -. DR OrthoDB; 479at2759; -. DR GO; GO:0005737; C:cytoplasm; 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 NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03148}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148, ECO:0000256|RuleBase:RU003781}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03148}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_03148}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148}. FT BINDING 8..13 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 38 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 50 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 66..67 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 143..146 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 166 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 171..172 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" SQ SEQUENCE 189 AA; 21073 MW; F2A738AA39269B1C CRC64; MTTITFVTGN ANKLKEFIQI LGKNFPYKLI NENIDIPEYQ GESDDISRAK CLEAAKIVKG PVVVEDTSLC FNALGGLPGP YIKWFLDKLK PEGLHHLLHG FEDKSAYALC TLAFSTGNLE TPVLLFKGQT DGKIVEPSGP NDFGWDPCFQ PDGFDQTYAE MPKELKNSLS HRGKAVMAFK EHFMNKTLK //