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
Mutation of Gly51 to serine in the P-loop of Lactobacillus casei folylpolyglutamate synthetase abolishes activity by altering the conformation of two adjacent loops.
Smith, C.A., Cross, J.A., Bognar, A.L., Sun, X.
Acta Crystallogr.,Sect.D