ID I3IRB1_9PLAN Unreviewed; 210 AA. AC I3IRB1; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 03-APR-2013, entry version 7. DE RecName: Full=Non-canonical purine NTP pyrophosphatase; DE EC=3.6.1.19; DE AltName: Full=Non-standard purine NTP pyrophosphatase; DE AltName: Full=Nucleoside-triphosphate diphosphatase; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase; GN ORFNames=KSU1_D0947; OS planctomycete KSU-1. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae. OX NCBI_TaxID=247490; RN [1] RP NUCLEOTIDE SEQUENCE. 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 RT nitrite reductase instead of a NirS-type with cytochrome cd1."; RL FEBS Lett. 586:1658-1663(2012). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions (By similarity). CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. CC -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use CC either magnesium or manganese (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 EnsemblBacteria; GAB64256; GAB64256; KSU1_D0947. 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:HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1; -. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR020922; Nucleoside-triphosphatase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT REGION 17 22 Substrate binding (By similarity). FT REGION 80 81 Substrate binding (By similarity). FT METAL 51 51 Magnesium or manganese (By similarity). FT METAL 80 80 Magnesium or manganese (By similarity). FT BINDING 166 166 Substrate (By similarity). FT BINDING 186 186 Substrate (By similarity). FT BINDING 192 192 Substrate (By similarity). 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 //