ID A0A2X1D935_BREVE Unreviewed; 200 AA. AC A0A2X1D935; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 16-JAN-2019, entry version 5. 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=NCTC11166_02762 {ECO:0000313|EMBL:SPU55366.1}; OS Brevundimonas vesicularis (Pseudomonas vesicularis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=41276 {ECO:0000313|EMBL:SPU55366.1, ECO:0000313|Proteomes:UP000251186}; RN [1] {ECO:0000313|EMBL:SPU55366.1, ECO:0000313|Proteomes:UP000251186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC11166 {ECO:0000313|EMBL:SPU55366.1, RC ECO:0000313|Proteomes:UP000251186}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) 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 --------------------------------------------------------------------------- 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; UAQP01000014; SPU55366.1; -; Genomic_DNA. DR Proteomes; UP000251186; Unassembled WGS sequence. 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-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 Complete proteome {ECO:0000313|Proteomes:UP000251186}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407, KW ECO:0000313|EMBL:SPU55366.1}; 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 15 20 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 158 161 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 186 187 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT ACT_SITE 75 75 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 46 46 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 75 75 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 76 76 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 181 181 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. SQ SEQUENCE 200 AA; 21076 MW; 66E79C5A516176F7 CRC64; MNLKLIKGMR IVVATHNGGK VPEISALLGG NYELVTAGQL NLPEPDETES TFTGNAMLKA RHAAELSGEV SLADDSGLSV AALDGAPGIF SARWAGPGKD FAVAMKKVEE RLEEIGATDR TAWFTSALAV AWPDGPCVVV QGEVHGQLTF PPRGDRGFGY DPLFIPNGGD RTFGEMEPAA KDAISHRTVA FAKLTAALID //