ID A0A2V8RX96_9BACT Unreviewed; 197 AA. AC A0A2V8RX96; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 05-DEC-2018, entry version 4. 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 Name=rdgB {ECO:0000313|EMBL:PYS91329.1}; GN ORFNames=DMF62_02675 {ECO:0000313|EMBL:PYS91329.1}; OS Acidobacteria bacterium. OC Bacteria; Acidobacteria. OX NCBI_TaxID=1978231 {ECO:0000313|EMBL:PYS91329.1}; RN [1] {ECO:0000313|EMBL:PYS91329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Gp4 AA14 {ECO:0000313|EMBL:PYS91329.1}; RX PubMed=29899444; DOI=.1038/s41586-018-0207-y; RA Crits-Christoph A., Diamond S., Butterfield C.N., Thomas B.C., RA Banfield J.F.; RT "Novel soil bacteria possess diverse genes for secondary metabolite RT biosynthesis."; RL Nature 558:440-444(2018). 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 -!- 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PYS91329.1}. 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; QHXS01000035; PYS91329.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. 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: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; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407}; 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 7 12 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 153 156 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 181 182 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT COILED 92 112 {ECO:0000256|SAM:Coils}. FT ACT_SITE 69 69 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 40 40 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 69 69 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 70 70 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 176 176 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 197 AA; 21696 MW; 5BC5B74413F73416 CRC64; MKILIATKNE GKIAELRSLL SDERHEFIGL DALSDIPDVE ETGNTFAENA KLKAAAYSTH FGLHTLADDS GLEVQALNGR PGVFSARYGG VKKNYDAKIR LLLEQLDEAE NKDRRARFVS HIAFASPNGD VLFEAEGVCE GSIAFKPKGT NGFGYDPVFI PAGFDQTFGE LSDQVKQKTS HRARAIAKIM RYLRDFA //