Serine hydroxymethyltransferase-like domain (IPR039429)

Short name: SHMT-like_dom

Overlapping homologous superfamilies

Domain relationships



Proteins containing this domain include serine hydroxymethyltransferase and fluorothreonine transaldolase.

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].

Fluorothreonine transaldolase catalyzes the final step in 4-fluorothreonine biosynthesis. It mediates a L-threonine/fluoroaceldehyde to 4-fluoro-L-threonine/acetaldehyde crossover reaction. It shares protein sequence similarity with SHMT [PMID: 19101471].

Contributing signatures

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