InterPro domain: IPR036637

A number of enzymes that catalyze the transfer of a phosphoryl group fromphosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shownto be structurally related [ 1 , 2 , 3 , 4 ]. All these enzymes share the same catalytic mechanism: they bind PEP andtransfer the phosphoryl group from it to a histidine residue. This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it [ 5 ].

1. Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Protein Sci. 2, 506-21
2. Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain. Gene 181, 103-8
3. Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs. Biochemistry 29, 10757-65
4. Temperature sensitivity of the cdc9-1 allele of Saccharomyces cerevisiae DNA ligase is dependent on specific combinations of amino acids in the primary structure of the expressed protein. Mol. Gen. Genet. 232, 332-4
5. The 3.0 A resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei. J. Mol. Biol. 318, 1417-32