ID A0A1X6Z7H6_9RHOB Unreviewed; 204 AA. AC A0A1X6Z7H6; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 30-AUG-2017, entry version 2. 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=RUM8411_01950 {ECO:0000313|EMBL:SLN43186.1}; OS Ruegeria meonggei. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=1446476 {ECO:0000313|EMBL:SLN43186.1, ECO:0000313|Proteomes:UP000193778}; RN [1] {ECO:0000313|EMBL:SLN43186.1, ECO:0000313|Proteomes:UP000193778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 8411 {ECO:0000313|EMBL:SLN43186.1, RC ECO:0000313|Proteomes:UP000193778}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of CC nucleoside triphosphates to their monophosphate derivatives, with CC a high preference for the non-canonical purine nucleotides XTP CC (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and CC ITP. Seems to function as a house-cleaning enzyme that removes CC non-canonical purine nucleotides from the nucleotide pool, thus CC preventing their incorporation into DNA/RNA and avoiding CC chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00805977}. CC -!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805978}. CC -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805983}. CC -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805979}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00730484}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00730348}. 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; FWFP01000005; SLN43186.1; -; Genomic_DNA. DR Proteomes; UP000193778; Unassembled WGS sequence. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-EC. 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; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000193778}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407, KW ECO:0000313|EMBL:SLN43186.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730390}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730432}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730340}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730332}. FT REGION 14 19 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 161 164 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 189 190 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT ACT_SITE 75 75 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 46 46 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 75 75 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 76 76 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 184 184 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 204 AA; 22145 MW; 8A7880E97D2D4BCC CRC64; MTRKFDGDRL LVATHNKGKL EEMAHLLSPF GVSVVGAGEM NLPEPEETED TFVGNARIKA HAAAKATGLP ALSDDSGITI DALDGAPGVY TADWAETGNG RDFLMAMTRA YTELEAKGAA HPRTAQFRST LVLAWPDGHD EVFEGIAPGH LVWPIRGEGG FGYDPMFVPE GHDITFAEMD RWEKNKISHR GRAVDMFVKG CFDG //