ID F8LBA9_9CHLA Unreviewed; 200 AA. AC F8LBA9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-MAY-2013, entry version 6. 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 Name=hamA; ORFNames=WCH_BS10310; OS Waddlia chondrophila 2032/99. OC Bacteria; Chlamydiae; Chlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=765953; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2032/99; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., RA Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S., RA Friedman M.G., Rattei T., Myers G.S.A., Horn M.; RT "Unity in variety -- the pan-genome of the Chlamydiae."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; FR872638; CCB90773.1; -; Genomic_DNA. 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; NTPase. 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 7 12 Substrate binding (By similarity). FT REGION 70 71 Substrate binding (By similarity). FT METAL 41 41 Magnesium or manganese (By similarity). FT METAL 70 70 Magnesium or manganese (By similarity). FT BINDING 156 156 Substrate (By similarity). FT BINDING 176 176 Substrate (By similarity). FT BINDING 182 182 Substrate (By similarity). SQ SEQUENCE 200 AA; 22620 MW; 30CDEA02925288CA CRC64; MELILATHNL HKIREFRQIL KEVKGLDLIS LRNFPDYQLP EETGKTFQEN ADLKALHAAK MLKAIVLADD SGLVVPALQG APGIYSARYA SSDATDKENR EKLMQEMEKF EDLDRSAYYE CCITIAGPEG ILKTAKATCE GLIGEQEKGR NGFGYDPIFI KHDYDKTFAE LEEQTKNRIS HRRKALDKIL AFLEAQIPSE //