ID I3IRB1_9PLAN Unreviewed; 210 AA. AC I3IRB1; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JAN-2015, entry version 16. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101763}; DE EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101728}; 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}; GN ORFNames=KSU1_D0947 {ECO:0000313|EMBL:GAB64256.1}; OS planctomycete KSU-1. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae. OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB64256.1}; RN [1] {ECO:0000313|EMBL:GAB64256.1} 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. {ECO:0000256|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00101772}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00174646}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00174646}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|SAAS:SAAS00174646}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00101722}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781}. 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: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 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 {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00101735}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00101759}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00101767}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00101755}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00101739}. FT REGION 17 22 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 80 81 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 51 51 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT METAL 80 80 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 192 192 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //