ID IXTPA_RHORT Reviewed; 201 AA. AC Q2RN61; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 28-FEB-2018, entry version 75. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=Rru_A3640; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) 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:0000255|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC 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; CP000230; ABC24434.1; -; Genomic_DNA. DR RefSeq; WP_011391387.1; NC_007643.1. DR RefSeq; YP_428721.1; NC_007643.1. DR ProteinModelPortal; Q2RN61; -. DR SMR; Q2RN61; -. DR STRING; 269796.Rru_A3640; -. DR EnsemblBacteria; ABC24434; ABC24434; Rru_A3640. DR GeneID; 3837096; -. DR KEGG; rru:Rru_A3640; -. DR PATRIC; fig|269796.9.peg.3762; -. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; YDPIFQP; -. DR OrthoDB; POG091H02BP; -. DR BioCyc; RRUB269796:GCN1-3695-MONOMER; -. DR Proteomes; UP000001929; Chromosome. 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:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. 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_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; Hydrolase; Magnesium; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 201 dITP/XTP pyrophosphatase. FT /FTId=PRO_1000087380. FT REGION 16 21 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 158 161 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 186 187 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT ACT_SITE 77 77 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 48 48 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 77 77 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 78 78 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT BINDING 181 181 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. SQ SEQUENCE 201 AA; 20884 MW; C339D1A4D7F47802 CRC64; MAMSRRLVES PLVVASHNAG KVREIAELIA PFGLEARSAA SLDLPEPEET GSSFVENALL KAHAAARATG LPALADDSGL AVSALGGDPG IYSARWAGPT KDFALAMATI NHLLGDNPDR SAHFVCALAL AWPDGHAETF EGRVDGVLVW PPRGDQGFGY DPMFLGEGAA ETFGEMDPAA KHAISHRARA FALLVAACLG G //