ID A0A3N4KMP6_9PEZI Unreviewed; 263 AA. AC A0A3N4KMP6; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 27-NOV-2024, entry version 24. 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=P167DRAFT_536424 {ECO:0000313|EMBL:RPB11770.1}; OS Morchella conica CCBAS932. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes; OC Pezizales; Morchellaceae; Morchella. OX NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB11770.1, ECO:0000313|Proteomes:UP000277580}; RN [1] {ECO:0000313|EMBL:RPB11770.1, ECO:0000313|Proteomes:UP000277580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB11770.1, RC ECO:0000313|Proteomes:UP000277580}; RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4; RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A., RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M., RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B., RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A., RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C., RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L., RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S., RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M., RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.; RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal RT truffle lifestyle."; RL Nat. Ecol. Evol. 2:1956-1965(2018). 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=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=3.6.1.9; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148}; 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=3.6.1.9; 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 EMBL; ML119133; RPB11770.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3N4KMP6; -. DR STRING; 1392247.A0A3N4KMP6; -. DR InParanoid; A0A3N4KMP6; -. DR Proteomes; UP000277580; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; 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 FunFam; 3.90.950.10:FF:000003; Inosine triphosphate pyrophosphatase; 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03148}; 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|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_03148}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}; KW Reference proteome {ECO:0000313|Proteomes:UP000277580}. FT REGION 182..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 10..15 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 51 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 67..68 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 142..145 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 163 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" FT BINDING 168..169 FT /ligand="ITP" FT /ligand_id="ChEBI:CHEBI:61402" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148" SQ SEQUENCE 263 AA; 28241 MW; B21226B320C20897 CRC64; MSSRTLFFVT SNPGKLAEAK AILSASGVNL ESKNVEITEI QGTIEEITRD KAKRAAEQIG GPVIVEDTCL CFDALKGLPG PYVKHFLKEI GTRGLTNMLA AYDDKTAQAV CTFAYCEPGS EPILFEGRTK GKVVRARGEG SFGWDPIFEY EGSTYAEMDS YQKNKISHRF KALQKLTAWL EEKHGGGSGG SGGSAPPPAA PKPVDRRNMG GHDTSSDGGS FFDGFGEEVK SRAINIAGDG MGIRKAAGRE WQFDSPDGGR GKY //