ID A0A8B8UUE3_SACPA Unreviewed; 197 AA. AC A0A8B8UUE3; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 08-NOV-2023, entry version 9. 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 Name=HAM1 {ECO:0000256|HAMAP-Rule:MF_03148}; GN ORFNames=SPAR_J02510 {ECO:0000313|RefSeq:XP_033767331.1}; OS Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=27291 {ECO:0000313|RefSeq:XP_033767331.1}; RN [1] {ECO:0000313|RefSeq:XP_033767331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033767331.1}; RX PubMed=28416820; RA Yue J.X., Li J., Aigrain L., Hallin J., Persson K., Oliver K., RA Bergstrom A., Coupland P., Warringer J., Lagomarsino M.C., Fischer G., RA Durbin R., Liti G.; RT "Contrasting evolutionary genome dynamics between domesticated and wild RT yeasts."; RL Nat. Genet. 49:913-924(2017). RN [2] {ECO:0000313|RefSeq:XP_033767331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033767331.1}; RA Yue J.-X.; RT "Population-level Yeast Reference Genomes."; RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|RefSeq:XP_033767331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033767331.1}; RG NCBI Genome Project; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|RefSeq:XP_033767331.1} RP IDENTIFICATION. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033767331.1}; RG RefSeq; RL Submitted (JUL-2023) to UniProtKB. 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. {ECO:0000256|HAMAP- CC 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 Nucleus {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 RefSeq; XP_033767331.1; XM_033911440.1. DR KEGG; spao:SPAR_J02510; -. DR VEuPathDB; FungiDB:SPAR_J02510; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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|ARBA:ARBA00023211, 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}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}. FT BINDING 10..15 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 45 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 58 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 76..77 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 76 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 151..154 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 175 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 180..181 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" SQ SEQUENCE 197 AA; 22011 MW; 83BD756B0D801939 CRC64; MGNNEIVFVT GNANKLKEVQ SILIQDVDSN NKTIHLINEA LDLEELQDTD LNAIALAKGK QAVAVLGKGK PVFVEDTALR FDEFNGLPGA YIKWFLKSMG LDKIVKMLEP FENKNAEAVT TICFADSRGE YHFFQGITKG KIVPSRGPTT FGWDSIFEPF DSNGLTYAEM TKDAKNAISH RGKAFAQFKE YLYQNDF //