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-MAY-2016, entry version 22. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020486}; DE EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020468}; 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}; GN ORFNames=PMI24_02017 {ECO:0000313|EMBL:EJM28855.1}; OS Pseudomonas sp. GM25. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144327 {ECO:0000313|EMBL:EJM28855.1, ECO:0000313|Proteomes:UP000007510}; RN [1] {ECO:0000313|EMBL:EJM28855.1, ECO:0000313|Proteomes:UP000007510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM25 {ECO:0000313|EMBL:EJM28855.1, RC ECO:0000313|Proteomes:UP000007510}; 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. {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 ECO:0000256|SAAS:SAAS00020483}. 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 ECO:0000256|SAAS:SAAS00020467}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00542593}. 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:EJM28855.1}. 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; AKJQ01000033; EJM28855.1; -; Genomic_DNA. DR RefSeq; WP_007953366.1; NZ_AKJQ01000033.1. DR EnsemblBacteria; EJM28855; EJM28855; PMI24_02017. DR Proteomes; UP000007510; 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-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 Complete proteome {ECO:0000313|Proteomes:UP000007510}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00425982}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425988}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00426004}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425941}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425996}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425966}. FT REGION 11 16 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 71 72 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 42 42 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT METAL 71 71 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 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 //