Aldh1l1
Domain
The N-terminal hydrolase domain has an NADP-independent formyltetrahydrofolate hydrolase activity, releasing formate and tetrahydrofolate.
The C-terminal aldehyde dehydrogenase domain has an NADP-dependent dehydrogenase activity. It catalyzes the oxidation of formate, released by the hydrolysis of formyltetrahydrofolate, into CO2.
The carrier domain is phosphopantetheinylated and uses the 4'-phosphopantetheine/4'-PP swinging arm to transfer the formyl group released by the N-terminal formyltetrahydrofolate hydrolase activity to the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP-dependent oxidation into CO2. The overall NADP-dependent physiological reaction requires the 3 domains (N-terminal hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to convert formyltetrahydrofolate into tetrahydrofolate and CO2.
Function
Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide (PubMed:31624291). May also have an NADP(+)-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde (By similarity).
Post-translational modifications
Phosphopantetheinylation at Ser-354 by AASDHPPT is required for the formyltetrahydrofolate dehydrogenase activity.
Sequence Similarities
In the N-terminal section; belongs to the GART family.
In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.
Tissue Specificity
Highly expressed in liver (at protein level) (PubMed:31624291). Also expressed in pancreas, brain and lung (at protein level) (PubMed:31624291).
Cellular localization
- Cytoplasm
- Cytosol
Alternative names
Fthfd, Aldh1l1, Cytosolic 10-formyltetrahydrofolate dehydrogenase, 10-FTHFDH, FDH, Aldehyde dehydrogenase family 1 member L1