{PDOC01029} {PS01326; DAP_EPIMERASE} {BEGIN} *************************************** * Diaminopimelate epimerase signature * *************************************** Diaminopimelate epimerase (EC 5.1.1.7) catalyzes the isomeriazation of L,L- to D,L-meso-diaminopimelate in the biosynthetic pathway leading from aspartate to lysine. This enzyme is a protein of about 30 Kd. Two conserved cysteines seem [1] to function as the acid and base in the catalytic mechanism. As a signature pattern, we selected the region surrounding the first of these two active site cysteines. -Consensus pattern: N-x-[DN]-[GS]-[SENGFT]-x(4)-C-[GI]-N-[GA]-x-R [C is an active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for an Anabaena dapF which has a Ser instead of the active site Cys. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2006 / Pattern revised. [ 1] Cirilli M., Zheng R., Scapin G., Blanchard J.S. "Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase." Biochemistry 37:16452-16458(1998). PubMed=9843410; DOI=10.1021/bi982138o -------------------------------------------------------------------------------- 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}