ID J3FAM8_9PSED Unreviewed; 198 AA. AC J3FAM8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 28-NOV-2012, entry version 3. 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; OS Pseudomonas sp. GM25. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144327; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM25; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.-Y.S., Schadt C.W., Pelletier D.A., Doktycz M.J.; RT "Sequencing of Twenty One Pseudomonas Genomes and Twenty Two Genomes RT from Diverse Bacteria isolated from Populus deltoides endosphere RT communities."; RL Submitted (MAY-2012) 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 (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 GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1; -. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR020922; Nucleoside-triphosphatase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 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 similarity). FT METAL 71 71 Magnesium or manganese (By similarity). FT BINDING 158 158 Substrate (By similarity). FT BINDING 178 178 Substrate (By similarity). FT BINDING 184 184 Substrate (By similarity). 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 //