{PDOC00090} {PS00096; SHMT} {BEGIN} *********************************************************************** * Serine hydroxymethyltransferase pyridoxal-phosphate attachment site * *********************************************************************** Serine hydroxymethyltransferase (EC 2.1.2.1) (SHMT) [1] catalyzes the transfer of the hydroxymethyl group of serine to tetrahydrofolate to form 5,10- methylenetetrahydrofolate and glycine. In vertebrates, it exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes. Serine hydroxymethyltransferase is a pyridoxal-phosphate containing enzyme. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme. -Consensus pattern: [DEQHY]-[LIVMFYA]-x-[GSTMVA]-[GSTAV]-[ST]-[STVM]-[HQ]-K- [STG]-[LFMI]-x-[GAS]-[PGAC]-[RQ]-[GSARH]-[GA] [K is the pyridoxal-P attachment site] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2006 / Pattern revised. [ 1] Usha R., Savithri H.S., Rao N.A. "The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases." Biochim. Biophys. Acta 1204:75-83(1994). PubMed=8305478 -------------------------------------------------------------------------------- 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}