ID RDGB_ECOLI Reviewed; 197 AA. AC P52061; Q2M9N9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 67. DE RecName: Full=Nucleoside-triphosphatase rdgB; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase; DE Short=NTPase; GN Name=rdgB; Synonyms=yggV; OrderedLocusNames=b2954, JW2921; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=12297000; RA Chung J.H., Park H.-Y., Lee J.H., Jang Y.; RT "Identification of the dITP- and XTP-hydrolyzing protein from RT Escherichia coli."; RL J. Biochem. Mol. Biol. 35:403-408(2002). RN [4] RP SUBSTRATE SPECIFICITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17090528; DOI=10.1074/jbc.M608708200; RA Burgis N.E., Cunningham R.P.; RT "Substrate specificity of RdgB protein, a deoxyribonucleoside RT triphosphate pyrophosphohydrolase."; RL J. Biol. Chem. 282:3531-3538(2007). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RG Midwest center for structural genomics (MCSG); RT "Putative ribosomal protein."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Hydrolyzes O6 atom-containing purine bases deoxyinosine CC triphosphate (dITP) and xanthosine triphosphate (XTP) as well as CC 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to CC nucleotide monophosphate and pyrophosphate. Probably excludes non- CC standard purines from DNA precursor pool, preventing thus CC incorporation into DNA and avoiding chromosomal lesions. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- COFACTOR: Divalent cations. Maximum activity is obtained with CC magnesium. Activity with manganese and nickel makes up 60-75% of CC the maximum rate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.33 mM for XTP; CC KM=0.36 mM for dITP; CC KM=0.41 mM for ITP; CC KM=16.5 uM for dHAPTP; CC Note=Vmax values are similar for XTP, dITP and ITP; CC pH dependence: CC Optimum pH is 10-10.5; CC -!- SUBUNIT: Homodimer. CC -!- MISCELLANEOUS: Activity toward dATP, dCTP and dTTP is less than 1% CC of the rate of XTP hydrolysis. Activity toward dGTP and dUTP is CC 10-12% lower than activity toward XTP. Modified or damaged CC nucleotides such as 6-chloropurine deoxyribose triphosphate, 8-Br- CC dGTP, 5-Br-dCTP, 5-Br-dUTP, 7-deaza-dGTP, 7-methyl-GTP, N6-etheno- CC ATP, NAD, NADH, FAD, ADP-ribose, UPD-glucose, AppA and ApppA are CC not hydrolyzed. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U28377; AAA69121.1; -; Genomic_DNA. DR EMBL; U00096; AAC75991.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77017.1; -; Genomic_DNA. DR PIR; A65081; A65081. DR RefSeq; AP_003511.1; -. DR RefSeq; NP_417429.1; -. DR PDB; 1K7K; X-ray; 1.50 A; A=1-197. DR PDB; 2PYU; X-ray; 2.02 A; A=1-197. DR PDB; 2Q16; X-ray; 1.95 A; A/B=1-197. DR PDBsum; 1K7K; -. DR PDBsum; 2PYU; -. DR PDBsum; 2Q16; -. DR DIP; DIP:12197N; -. DR GeneID; 947429; -. DR GenomeReviews; AP009048_GR; JW2921. DR GenomeReviews; U00096_GR; b2954. DR KEGG; ecj:JW2921; -. DR KEGG; eco:b2954; -. DR EchoBASE; EB2807; -. DR EcoGene; EG12982; rdgB. DR HOGENOM; P52061; -. DR OMA; P52061; VYTADWA. DR BioCyc; EcoCyc:G7530-MON; -. DR BioCyc; MetaCyc:G7530-MON; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:HAMAP. DR HAMAP; MF_01405; -; 1. DR InterPro; IPR002637; Ham1p-like. DR PANTHER; PTHR11067; Ham1p_like; 1. DR Pfam; PF01725; Ham1p_like; 1. DR TIGRFAMs; TIGR00042; Ham1p_like; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; KW Nickel. FT CHAIN 1 197 Nucleoside-triphosphatase rdgB. FT /FTId=PRO_0000178164. FT STRAND 2 7 FT HELIX 11 21 FT HELIX 22 24 FT STRAND 26 30 FT TURN 31 35 FT HELIX 46 61 FT STRAND 65 74 FT HELIX 75 77 FT HELIX 82 87 FT HELIX 95 106 FT HELIX 111 113 FT STRAND 115 127 FT STRAND 134 144 FT STRAND 152 154 FT HELIX 157 159 FT HELIX 163 165 FT STRAND 166 168 FT HELIX 169 171 FT HELIX 174 180 FT HELIX 182 193 SQ SEQUENCE 197 AA; 21039 MW; 74E82A59B1A9E294 CRC64; MQKVVLATGN VGKVRELASL LSDFGLDIVA QTDLGVDSAE ETGLTFIENA ILKARHAAKV TALPAIADDS GLAVDVLGGA PGIYSARYSG EDATDQKNLQ KLLETMKDVP DDQRQARFHC VLVYLRHAED PTPLVCHGSW PGVITREPAG TGGFGYDPIF FVPSEGKTAA ELTREEKSAI SHRGQALKLL LDALRNG //