ID A0A517W5M5_9BACT Unreviewed; 206 AA. AC A0A517W5M5; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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 ORFNames=V6x_02300 {ECO:0000313|EMBL:QDU00555.1}; OS Planctomycetes bacterium V6. OC Bacteria; Planctomycetes. OX NCBI_TaxID=2528030 {ECO:0000313|EMBL:QDU00555.1, ECO:0000313|Proteomes:UP000320722}; RN [1] {ECO:0000313|EMBL:QDU00555.1, ECO:0000313|Proteomes:UP000320722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V6 {ECO:0000313|EMBL:QDU00555.1, RC ECO:0000313|Proteomes:UP000320722}; RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., RA Rivas-Marin E., Kohn T., Peeters S.H., Heuer A., Rast P., RA Oberbeckmann S., Bunk B., Jeske O., Meyerdierks A., Storesund J.E., RA Kallscheuer N., Luecker S., Lage O.M., Pohl T., Merkel B.J., RA Hornburger P., Mueller R.-W., Bruemmer F., Labrenz M., Spormann A.M., RA Op den Camp H., Overmann J., Amann R., Jetten M.S.M., Mascher T., RA Medema M.H., Devos D.P., Kaster A.-K., Ovreas L., Rohde M., RA Galperin M.Y., Jogler C.; RT "Deep-cultivation of Planctomycetes and their phenomic and genomic RT characterization uncovers novel biology."; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}. 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; CP036347; QDU00555.1; -; Genomic_DNA. DR Proteomes; UP000320722; Chromosome. 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:UP000320722}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407, KW ECO:0000313|EMBL:QDU00555.1}; 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}. 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 73 73 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 73 73 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 74 74 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 206 AA; 22959 MW; C5BF1AB3095CACEA CRC64; MSHYPRIVLA SRNQKKAGEI AELLKPHGIE VQSVADFPQA QEVVEDGHSF AENAAKKAYE TAQAISEWTI GEDSGLMIDA LDGAPGIYSA RYSGENATDE KNNAKMLEEL KDVPLPERTA AYICNVALSN PQGEICLQVE ARCRGRMTDQ ARGENGFGYD PYFEIIELHK TFGELAPIVK QHLSHRARAF ERFIPQLVDL FHKLDD //