ID C5QRW4_9STAP Unreviewed; 201 AA. AC C5QRW4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 30-NOV-2016, entry version 41. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE EC=3.6.1.9 {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 AltName: Full=Nucleotide diphosphatase {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 hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions. {ECO:0000256|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {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 Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-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 PATRIC; 31395443; VBIStaEpi14170_0288. 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:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR CDD; cd00515; HAM1; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. 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 Manganese {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 74 75 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 45 45 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT METAL 74 74 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 158 158 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 178 178 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 184 184 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 //