Serine hydroxymethyltransferase (IPR001085)

Short name: Ser_HO-MeTrfase

Overlapping homologous superfamilies

Family relationships


This entry includes serine hydroxymethyltransferases and other uncharacterised proteins.

Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent enzyme that catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate [PMID: 11063567]. This reaction generates single carbon units for purine, thymidine, and methionine biosynthesis. It belongs to the aspartate aminotransferase superfamily (fold type I) [PMID: 10828359]. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme [PMID: 8305478]. 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 [PMID: 10828359, PMID: 11877399].

GO terms

Biological Process

GO:0019264 glycine biosynthetic process from serine
GO:0035999 tetrahydrofolate interconversion

Molecular Function

GO:0004372 glycine hydroxymethyltransferase activity
GO:0030170 pyridoxal phosphate binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.