ID J3FAM8_9PSED Unreviewed; 198 AA. AC J3FAM8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 11-JUN-2014, entry version 10. DE RecName: Full=Non-canonical purine NTP pyrophosphatase; DE EC=3.6.1.19; DE AltName: Full=Non-standard purine NTP pyrophosphatase; DE AltName: Full=Nucleoside-triphosphate diphosphatase; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase; GN ORFNames=PMI24_02017; OS Pseudomonas sp. GM25. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144327; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM25; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. CC -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use CC either magnesium or manganese (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AKJQ01000033; EJM28855.1; -; Genomic_DNA. DR EnsemblBacteria; EJM28855; EJM28855; PMI24_02017. 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-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 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 SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT REGION 11 16 Substrate binding (By similarity). FT REGION 71 72 Substrate binding (By similarity). FT METAL 42 42 Magnesium or manganese (By FT similarity){EA12}. FT METAL 71 71 Magnesium or manganese (By FT similarity){EA12}. FT BINDING 158 158 Substrate (By similarity){EA12}. FT BINDING 178 178 Substrate (By similarity){EA12}. FT BINDING 184 184 Substrate (By similarity){EA12}. SQ SEQUENCE 198 AA; 21239 MW; 091E6854921CE7A4 CRC64; MINLKQLVLA SHNAGKLKEL QAMLGESVQL RSIGEFSSVE PEETGLSFVE NAILKARNAA RISGLPALAD DSGLAVDFLG GAPGIYSARY ADGKGDAANN AKLLDALKDV PEAERGAQFV CVLALVRHAD DPLPILCEGL WHGRILTAAS GEHGFGYDPL FWVPERNVSS AELSPSDKNQ ISHRARAMDL LRQRLGLK //