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uvrA | Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (943 aa) | ||||
purT | Phosphoribosylglycinamide formyltransferase 2; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family. (402 aa) | ||||
gshB | Glutathione synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic GSH synthase family. (314 aa) | ||||
purK | 5-(carboxyamino)imidazole ribonucleotide synthase; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (373 aa) | ||||
sucC | succinate--CoA ligase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa) | ||||
purD | Phosphoribosylamine--glycine ligase; Catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GARS family. (427 aa) | ||||
AMW78593.1 | Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (792 aa) |