ID A0A7Z2YCT3_9VIBR Unreviewed; 196 AA. AC A0A7Z2YCT3; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 13-SEP-2023, entry version 9. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405}; GN ORFNames=GT360_02115 {ECO:0000313|EMBL:QIA62390.1}; OS Vibrio astriarenae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=1481923 {ECO:0000313|EMBL:QIA62390.1, ECO:0000313|Proteomes:UP000464262}; RN [1] {ECO:0000313|EMBL:QIA62390.1, ECO:0000313|Proteomes:UP000464262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HN897 {ECO:0000313|EMBL:QIA62390.1, RC ECO:0000313|Proteomes:UP000464262}; RA Liu Y., Zhao Z.; RT "Whole genome and functional gene identification of agarase of Vibrio RT HN897."; RL Submitted (JAN-2020) 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:0000256|HAMAP-Rule:MF_01405}. 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=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; 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=3.6.1.66; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|RuleBase:RU003781}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP047475; QIA62390.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Z2YCT3; -. DR KEGG; vas:GT360_02115; -. DR Proteomes; UP000464262; Chromosome 1. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01405}; Reference proteome {ECO:0000313|Proteomes:UP000464262}. FT ACT_SITE 69 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 8..13 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 154..157 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 182..183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" SQ SEQUENCE 196 AA; 21297 MW; D9E0C4BD23F48274 CRC64; MKKIVLATGN QGKVREMADL LSDFGFEVLA QSEFNVSDVA ETGTTFIENA IIKARHAAKE TGLAAIADDS GLEVDFLKGA PGIYSARYAG EGASDQQNLE KLLDAMKGVP EAERTARFHC VLVLMKHEND PTPIVCHGKW EGRILEKADG ENGFGYDPVF FVPEDNCSSA QLEPARKKQL SHRGKALTAL FAELSK //