ID K7A240_9ALTE Unreviewed; 200 AA. AC K7A240; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 03-JUL-2019, entry version 46. 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 Name=mazG {ECO:0000313|EMBL:GAC35008.1}; GN ORFNames=GPLA_4129 {ECO:0000313|EMBL:GAC35008.1}; OS Paraglaciecola polaris LMG 21857. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC35008.1, ECO:0000313|Proteomes:UP000006322}; RN [1] {ECO:0000313|EMBL:GAC35008.1, ECO:0000313|Proteomes:UP000006322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC35008.1, RC ECO:0000313|Proteomes:UP000006322}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC35008.1}. 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; BAER01000124; GAC35008.1; -; Genomic_DNA. DR RefSeq; WP_007106772.1; NZ_BAER01000124.1. DR EnsemblBacteria; GAC35008; GAC35008; GPLA_4129. DR OrthoDB; 1824064at2; -. DR Proteomes; UP000006322; 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:UP000006322}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407, KW ECO:0000313|EMBL:GAC35008.1}; 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 9 14 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 70 70 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT METAL 70 70 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 71 71 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 200 AA; 21492 MW; D7D7964716B6A2AE CRC64; MSRKIVLATG NKGKVAELSQ LLSPLDIDIV PQSEFNVPDV AETGTTFVEN AIIKARHAAK ITGLPAIADD SGLAVDALDG APGVYSARYA GSHATDTDNI DKLLEALKDV APAARHARFL CVLVYMRSAD DPTPIICQGE WHGKITTQRT GDSGFGYDPV FWVEQKQCTS AQLSKEQKNA LSHRGQALDQ LLITLSADFD //