ID D1CD51_THET1 Unreviewed; 202 AA. AC D1CD51; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 10-MAY-2017, entry version 55. 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=Tter_1810 {ECO:0000313|EMBL:ACZ42716.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42716.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). 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: ITP + H(2)O = IMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805978}. CC -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805983}. CC -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805979}. 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; CP001825; ACZ42716.1; -; Genomic_DNA. DR STRING; 525904.Tter_1810; -. DR EnsemblBacteria; ACZ42716; ACZ42716; Tter_1810. DR KEGG; ttr:Tter_1810; -. DR PATRIC; 32503944; VBITheTer68767_1937. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; POG091H02BP; -. DR BioCyc; TTER525904:GHMJ-1847-MONOMER; -. DR Proteomes; UP000000323; Chromosome 1. 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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-HAMAP. DR CDD; cd00515; HAM1; 1. 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:UP000000323}; 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:UP000000323}. FT REGION 10 15 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 155 158 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 183 184 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 178 178 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 202 AA; 22403 MW; 02A832DD1806E3B8 CRC64; MKLSKLLIAS DNPGKLAEYQ ELLSGLGIEI VSMRDAGIER APEETGSTFE ENALIKARYC WNMTGISSIA DDSGLEVAAL GGEPGVRSKR WAGEQISDAE RNKLLIERLN KASSSNKSAR FVCVIALIDR YGNEHLFRGE VEGVIIDHPR GSHGFGYDPI FYLPELGKTF AELDMLEKNR VSHRARAAQL AVDWIKRNLD KL //