Formate-tetrahydrofolate ligase

Formate--tetrahydrofolate ligase
the crystal structure of formyltetrahydrofolate synthetase from moorella thermoacetica
Identifiers
Symbol	FTHFS
Pfam	PF01268
Pfam clan	CL0023
InterPro	IPR000559
PROSITE	PDOC00595
SCOP	1fpm
SUPERFAMILY	1fpm
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a formate-tetrahydrofolate ligase (EC 6.3.4.3) is an enzyme that catalyzes the chemical reaction

The 3 substrates of this enzyme are ATP, formate, and tetrahydrofolate, whereas its 3 products are ADP, phosphate, and 10-formyltetrahydrofolate.

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.

In eukaryotes the FTHFS activity is expressed by a multifunctional enzyme, C-1-tetrahydrofolate synthase (C1-THF synthase), which also catalyses the dehydrogenase and cyclohydrolase activities. Two forms of C1-THF synthases are known, one is located in the , while the second one is cytoplasmic. In both forms the FTHFS domain consists of about 600 amino acid residues and is located in the C-terminal section of C1-THF synthase. In prokaryotes FTHFS activity is expressed by a monofunctional homotetrameric enzyme of about 560 amino acid residues.