|nudG||Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP. (135 aa)|| |
Predicted Functional Partners:
Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities . In vitro, can hydrolyze pppGp . Also has exopolyphosphatase activity, catalyzing the release of orthophosphate by processive hydrolysis of the phosphoanyhydride bonds of polyphosphate chains (1000 residues)
| || || || || || ||0.796
annotation not available
| || || || || || ||0.750
Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP)
| || || || || || ||0.622
Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell
| || || || || || || ||0.609
Inner membrane protein YnjF; Putative cytochrome oxidase
| || || || || || || ||0.603
Catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5- phosphate and the corresponding free base. Can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. Cannot catalyze the reverse reactions. Is required for optimal growth in glucose minimal medium, possibly because it contributes to nucleoside pool homeostasis by degrading excess nucleotides and feeding back the ribose moiety to catabolism.
| || || || || || ||0.582
Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate
| || || || ||0.503
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
| || || ||0.502
Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP
| || || || || || || ||0.487
Inducible lysine decarboxylase that catalyzes the proton- dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide . Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by- products of carbohydrate fermentation .
| || || || || || ||0.485