ID Q1QSA7_CHRSD Unreviewed; 201 AA. AC Q1QSA7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 22-JUL-2015, entry version 62. 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 OrderedLocusNames=Csal_3307 {ECO:0000313|EMBL:ABE60651.1}; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE60651.1, ECO:0000313|Proteomes:UP000000239}; RN [1] {ECO:0000313|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) 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 ECO:0000256|SAAS:SAAS00020483}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|SAAS:SAAS00167296}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|SAAS:SAAS00167296}; 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 ECO:0000256|SAAS:SAAS00167296}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+).; 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 --------------------------------------------------------------------------- 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; CP000285; ABE60651.1; -; Genomic_DNA. DR RefSeq; WP_011508597.1; NC_007963.1. DR ProteinModelPortal; Q1QSA7; -. DR SMR; Q1QSA7; 5-198. DR STRING; 290398.Csal_3307; -. DR EnsemblBacteria; ABE60651; ABE60651; Csal_3307. DR KEGG; csa:Csal_3307; -. DR PATRIC; 21450494; VBIChrSal113723_3324. DR eggNOG; COG0127; -. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG6CZQQP; -. DR Proteomes; UP000000239; Chromosome. 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:UP000000239}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00020482}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00020469}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00020489}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00020487}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00020485}; KW Reference proteome {ECO:0000313|Proteomes:UP000000239}. FT REGION 11 16 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 72 73 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 43 43 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT METAL 72 72 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 160 160 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 201 AA; 21804 MW; E9FC27509A7810D0 CRC64; MADQDTLVLA SGNTGKLREF QSLLAPLGLE VRPQRDFAVT EVEETGLTFV ENALLKAREA SRVSGLPALA DDSGLEVDAL QGAPGIRSAR FAGEPSDDAA NNRKLLEALK DVPEGQRGAR FWCVLVYLRH AEDPVPRIVQ CAWEGEVLAY PRGEGGFGYD SLFWVPERAM TAAELSAEDK NRLSHRGRAM QALLAQLSAP S //