ID I3IRB1_9BACT Unreviewed; 210 AA. AC I3IRB1; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 12-AUG-2020, entry version 42. 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=KSU1_D0947 {ECO:0000313|EMBL:GAB64256.1}; OS Candidatus Jettenia caeni. OC Bacteria; Planctomycetes; Candidatus Brocadiae; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Jettenia. OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB64256.1, ECO:0000313|Proteomes:UP000002985}; RN [1] {ECO:0000313|EMBL:GAB64256.1, ECO:0000313|Proteomes:UP000002985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041; RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M., RA Furukawa K., Fujii T.; RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite RT reductase instead of a NirS-type with cytochrome cd1."; RL FEBS Lett. 586:1658-1663(2012). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAB64256.1}. 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; BAFH01000004; GAB64256.1; -; Genomic_DNA. DR RefSeq; WP_007223336.1; NZ_BAFH01000004.1. DR STRING; 247490.KSU1_D0947; -. DR EnsemblBacteria; GAB64256; GAB64256; KSU1_D0947. DR eggNOG; COG0127; Bacteria. DR OrthoDB; 1824064at2; -. DR Proteomes; UP000002985; Unassembled WGS sequence. 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}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01405}; Reference proteome {ECO:0000313|Proteomes:UP000002985}. FT REGION 17..22 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 163..166 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 191..192 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT ACT_SITE 80 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 51 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 80 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 81 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 186 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" SQ SEQUENCE 210 AA; 23926 MW; 65C6D849B873BA2C CRC64; MTSITNDIHK KTILIATQNK NKRIEILDIL KNIPGILFRD IEDFPFLPTV EEDKNTFQEN AVKKATILAK ACNTWVMADD SGLQIDALNG RPGVFSCRYA GPNATDEKNR EKVLSELKGV PKERRTARFV CTIALASPHE LFFVVEGRCE GFITEEPKGK RGFGYDPIFY VPQYHQTFGE LHSSIKNMIS HRADALKQFK ERIMPLIRKI //