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-SEP-2014, entry version 12. 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 RefSeq; WP_007223336.1; NZ_BAFH01000004.1. 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:UniProtKB-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:UniProtKB-HAMAP. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. 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; 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 FT similarity){EA12}. FT METAL 80 80 Magnesium or manganese (By FT similarity){EA12}. FT BINDING 166 166 Substrate (By similarity){EA12}. FT BINDING 186 186 Substrate (By similarity){EA12}. FT BINDING 192 192 Substrate (By similarity){EA12}. 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 //