ID Q1QSA7_CHRSD Unreviewed; 201 AA. AC Q1QSA7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 13-FEB-2019, entry version 90. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {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 Short=NTPase {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|EMBL:ABE60651.1, 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}; RX PubMed=22675587; DOI=10.4056/sigs.2285059; RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., RA Detter J.C., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., RA Brettin T., Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., RA Kyrpides N.C., Ivanova N., Goker M., Klenk H.P., Csonka L.N., RA Woyke T.; RT "Complete genome sequence of the halophilic and highly halotolerant RT Chromohalobacter salexigens type strain (1H11(T))."; RL Stand. Genomic Sci. 5:379-388(2011). CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of CC nucleoside triphosphates to their monophosphate derivatives, with CC a high preference for the non-canonical purine nucleotides XTP CC (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and CC ITP. Seems to function as a house-cleaning enzyme that removes CC non-canonical purine nucleotides from the nucleotide pool, thus CC preventing their incorporation into DNA/RNA and avoiding CC chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00805977}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; CC Xref=Rhea:RHEA:29399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; CC EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS01118622}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; CC Xref=Rhea:RHEA:28610, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; CC EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS01118649}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); CC Xref=Rhea:RHEA:28342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; CC EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS01118637}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00730484}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00730348}. 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 STRING; 290398.Csal_3307; -. DR EnsemblBacteria; ABE60651; ABE60651; Csal_3307. DR KEGG; csa:Csal_3307; -. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; YDPIFQP; -. DR OrthoDB; 1824064at2; -. DR BioCyc; CSAL290398:G1GJB-3381-MONOMER; -. 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-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR020922; dITP/XTP_pyrophosphatase. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. 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, ECO:0000256|SAAS:SAAS00730407}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730390}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730432}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730340}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00730332}; KW Reference proteome {ECO:0000313|Proteomes:UP000000239}. FT REGION 11 16 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 157 160 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 185 186 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT ACT_SITE 72 72 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 43 43 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 72 72 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 73 73 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 180 180 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 //