ID Q1QSA7_CHRSD Unreviewed; 201 AA. AC Q1QSA7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 10-FEB-2021, entry version 106. 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 ATCC BAA-138 / DSM 3043 / CIP 106854 / OS NCIMB 13768 / 1H11). 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=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11 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., Detter J.C., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D., RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T., RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C., RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., 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 nucleoside CC triphosphates to their monophosphate derivatives, with a high CC preference for the non-canonical purine nucleotides XTP (xanthosine CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to CC function as a house-cleaning enzyme that removes non-canonical purine CC nucleotides from the nucleotide pool, thus preventing their CC incorporation into DNA/RNA and avoiding chromosomal lesions. CC {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405, CC 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 STRING; 290398.Csal_3307; -. DR EnsemblBacteria; ABE60651; ABE60651; Csal_3307. DR KEGG; csa:Csal_3307; -. DR eggNOG; COG0127; Bacteria. DR HOGENOM; CLU_082080_0_3_6; -. DR OMA; YDPIFQP; -. DR OrthoDB; 1824064at2; -. DR BioCyc; CSAL290398:G1GJB-3381-MONOMER; -. DR Proteomes; UP000000239; Chromosome. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC. 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01405}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01405}; Reference proteome {ECO:0000313|Proteomes:UP000000239}. FT REGION 11..16 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 157..160 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 185..186 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 43 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 72 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 73 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 180 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule: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 //