The domain within your query sequence starts at position 20 and ends at position 408; the E-value for the SHMT domain shown below is 4.6e-196.



PFAM accession number:PF00464
Interpro abstract (IPR039429):

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 [ (PUBMED:11063567) ]. This reaction generates single carbon units for purine, thymidine, and methionine biosynthesis. It belongs to the aspartate aminotransferase superfamily (fold type I) [ (PUBMED:10828359) ]. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme [ (PUBMED: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 [ (PUBMED:10828359) (PUBMED: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 [ (PUBMED:19101471) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SHMT