CATH Classification

Domain Context

CATH Clusters

Superfamily Mur-like, catalytic domain
Functional Family

Enzyme Information
Tetrahydrofolate synthase.
based on mapping to UniProt P15925
ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
-!- In some bacteria, a single protein catalyzes both this activity and that of EC, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates (H(4)folate). -!- In contrast, the activities are located on separate proteins in most eukaryotes studied to date. -!- In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. -!- Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes. -!- As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C(1) metabolism. -!- The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.

UniProtKB Entries (1)

Lactobacillus casei
Folylpolyglutamate synthase

PDB Structure

External Links
Organism Escherichia
Primary Citation
Folate-binding triggers the activation of folylpolyglutamate synthetase.
Sun, X., Cross, J.A., Bognar, A.L., Baker, E.N., Smith, C.A.