ID A0A517W5M5_9BACT Unreviewed; 206 AA. AC A0A517W5M5; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 11-DEC-2019, entry version 3. 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., Rivas-Marin E., RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B., RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S., RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F., RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R., RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K., RA Ovreas L., Rohde M., 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 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, ECO:0000256|SAAS:SAAS00805977}. 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 ECO:0000256|SAAS:SAAS01118622}; 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 ECO:0000256|SAAS:SAAS01118649}; 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 ECO:0000256|SAAS:SAAS01118637}; 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 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 of CC 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|RuleBase:RU003781, KW ECO:0000256|SAAS:SAAS00730407, ECO:0000313|EMBL:QDU00555.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, 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 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 73 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 73 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 74 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 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 //