ID C5QRW4_9STAP Unreviewed; 201 AA. AC C5QRW4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 20-JUN-2018, entry version 49. 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:EES40348.1}; GN ORFNames=HMPREF0793_1825 {ECO:0000313|EMBL:EES40348.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES40348.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES40348.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES40348.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) 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 -!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405}. 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 -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781}. 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:EES40348.1}. 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; ACJB01000060; EES40348.1; -; Genomic_DNA. DR STRING; 525378.HMPREF0793_1825; -. DR EnsemblBacteria; EES40348; EES40348; HMPREF0793_1825. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR OrthoDB; POG091H02BP; -. DR Proteomes; UP000003152; Unassembled WGS sequence. 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 TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003152}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000313|EMBL:EES40348.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405}; KW Reference proteome {ECO:0000313|Proteomes:UP000003152}. FT REGION 14 19 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 155 158 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 183 184 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT ACT_SITE 74 74 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 45 45 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 74 74 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 75 75 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 178 178 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 201 AA; 22276 MW; E1BC27F5C0876FED CRC64; MGEPMTMEDI VIATNNQGKI NDFKAIFKDD HVIGISELIQ DFDVEETGTT FEENAILKSE AAAKALNKRV IADDSGLEVF ALDGEPGVYS ARYAGLDKSD DANIDKLLSN LENESDRRAQ FVCVISMSAP DEETKTFKGT VSGEITRERR GENGFGYDPV FFVPDKDRTM AEISNEEKSK ISHRSNAIQK LNAYLEGENH V //