v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | This conserved region is found in four-carbon acid sugar kinases from a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. These four-carbon acid sugar kinases are composed of two domains: an N-terminal domain and a C-terminal domain connected by a variable linker sequence. The N-terminal domain exhibits an α/β-fold composed of an eight-stranded parallel β-sheet. The C-terminal domain also exhibits an α/β-fold composed of a seven-stranded mixed β-sheet. The acid sugar is bound by the N-terminal domain, while nucleotide by the C-terminal domain [ ].Proteins containing this domain include D-threonate kinase from Salmonella typhimurium (DtnK), 3-oxo-tetronate kinase from Methylobacterium radiotolerans, 3-oxo-isoapionate kinase from Paraburkholderia graminis and D-erythronate kinase from Heliobacterium modesticaldum. DtnK catalyzes the ATP-dependent phosphorylation of D-threonate to D-threonate 4-phosphate and is also able to phosphorylate 4-hydroxy-L-threonine, which may serve to deal with the toxicity of this compound [ , ]. |
Short Name | 4-carb_acid_sugar_kinase_N |