{PDOC51554} {PS51554; PFL} {BEGIN} *********************************************** * Pyruvate formate lyase (PFL) domain profile * *********************************************** Pyruvate formate lyase (PFL) catalyzes the non-oxidative conversion of pyruvate and CoA to formate and acetyl-CoA. Several other enzymes have been identified in the pyruvate formate lyase family: ketoacid formate lyase, glycerol dehydratase (GD), benzyl succinate synthetase and p-hydroxyphenylacetate decarboxylase [1,2]. The PFL domain has a unique alpha/beta barrel arrangement, with five 'up' strands and three 'down' strands; the up and down strands are linked by a unique beta finger that carries a key thiyl radical (see ) [1,2]. The profile we developed covers the entire PFL domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2011 / First entry. [ 1] Leppaenen V.-M., Merckel M.C., Ollis D.L., Wong K.K., Kozarich J.W., Goldman A. "Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase." Structure 7:733-744(1999). PubMed=10425676 [ 2] Lehtioe L., Grossmann J.G., Kokona B., Fairman R., Goldman A. "Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus." J. Mol. Biol. 357:221-235(2006). PubMed=16414072; DOI=10.1016/j.jmb.2005.12.049 -------------------------------------------------------------------------------- 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}