Description

IPR019798 is a Serine hydroxymethyltransferase, pyridoxal phosphate binding site.

<p>Synonym(s): Serine hydroxymethyltransferase, Serine aldolase, Threonine aldolase <p>Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) dependent enzyme and belongs to the aspartate aminotransferase superfamily (fold type I) [[cite:PUB00014432]]. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme [[cite:PUB00000663]]. The enzyme carries out interconversion of serine and glycine using PLP as the cofactor. SHMT catalyses the transfer of a hydroxymethyl group from N5, N10- methylene tetrahydrofolate to glycine, resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers and the mammalian enzyme forms a homotetramer [[cite:PUB00014432], [cite:PUB00014439]]. PLP dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalysed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), D-amino acid superfamily (fold type IV) and glycogen phophorylase family (fold type V) [[cite:PUB00006301], [cite:PUB00006322]].</p> <p>In vertebrates, glycine hydroxymethyltransferase exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes.</p> <p>The signature of this entry contains the lysine residue to which the pyridoxal phosphate group is attached. The region surrounding this lysine residue is highly conserved in all forms of the enzyme.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 28

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: