ID NTPA_RHORT Reviewed; 201 AA. AC Q2RN61; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.19 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=Rru_A3640; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) 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. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. 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; CP000230; ABC24434.1; -; Genomic_DNA. DR RefSeq; WP_011391387.1; NC_007643.1. DR RefSeq; YP_428721.1; NC_007643.1. DR ProteinModelPortal; Q2RN61; -. DR STRING; 269796.Rru_A3640; -. DR EnsemblBacteria; ABC24434; ABC24434; Rru_A3640. DR GeneID; 3837096; -. DR KEGG; rru:Rru_A3640; -. DR PATRIC; 23331090; VBIRhoRub82919_3762. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG65QWHX; -. DR BioCyc; RRUB269796:GCN1-3704-MONOMER; -. DR Proteomes; UP000001929; Chromosome. 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 Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 201 Non-canonical purine NTP pyrophosphatase. FT /FTId=PRO_1000087380. FT REGION 16 21 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 77 78 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 48 48 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT METAL 77 77 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT BINDING 161 161 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 181 181 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 187 187 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. SQ SEQUENCE 201 AA; 20884 MW; C339D1A4D7F47802 CRC64; MAMSRRLVES PLVVASHNAG KVREIAELIA PFGLEARSAA SLDLPEPEET GSSFVENALL KAHAAARATG LPALADDSGL AVSALGGDPG IYSARWAGPT KDFALAMATI NHLLGDNPDR SAHFVCALAL AWPDGHAETF EGRVDGVLVW PPRGDQGFGY DPMFLGEGAA ETFGEMDPAA KHAISHRARA FALLVAACLG G //