{PDOC00460} {PS00532; PEPCK_ATP} {BEGIN} ***************************************************** * Phosphoenolpyruvate carboxykinase (ATP) signature * ***************************************************** Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) (PEPCK) [1] catalyzes the formation of phosphoenolpyruvate by decarboxylation of oxaloacetate while hydrolyzing ATP, a rate limiting step in gluconeogenesis (the biosynthesis of glucose). The sequence of this enzyme has been obtained from Escherichia coli, yeast, and Trypanosoma brucei; these three sequences are evolutionary related and share many regions of similarity. As a signature pattern we selected a highly conserved region that contains four acidic residues and which is located in the central part of the enzyme. The beginning of the pattern is located about 10 residues to the C-terminus of an ATP-binding motif 'A' (P-loop) (see ) and is also part of the ATP-binding domain [2]. -Consensus pattern: L-I-G-D-D-E-H-x-W-x-[DEPKVNA]-x-[GVS]-[IV]-x-N -Sequences known to belong to this class detected by the pattern: ALL, except for Staphylococcus aureus PEPCK. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: Phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) an enzyme that catalyzes the same reaction, but using GTP instead of ATP, is not related to the above enzyme (see ). -Last update: April 2006 / Pattern revised. [ 1] Medina V., Pontarollo R., Glaeske D., Tabel H., Goldie H. "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae." J. Bacteriol. 172:7151-7156(1990). PubMed=1701430 [ 2] Matte A., Goldie H., Sweet R.M., Delbaere L.T.J. "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold." J. Mol. Biol. 256:126-143(1996). PubMed=8609605 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}