InterPro : IPR011407

Name  10-formyltetrahydrofolate dehydrogenase Short Name  10_FTHF_DH
Type  Family Description  This group represents a 10-formyltetrahydrofolate dehydrogenase (FDH). This enzyme catalyses the reaction: 10-formyltetrahydrofolate + H2O + NADP+ = tetrahydrofolate + CO2 + NADPH + H+ As such it acts as an NADP-dependent aldehyde dehydrogenase []. It is composed of two catalytic domains (the N- and C-terminal domains), which are connected by a 100-amino acid residue linker (intermediate domain). The intermediate domain functions similarly to an acyl carrier protein by binding to 4'-phosphopantetheine []. FDH differs from other members of the aldehyde dehydrogenase family in that it binds the 2'-phosphate group of NADP via a water-mediated contact with Gln600, which may contribute to the specificity of the enzyme for NADP over NAD [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

7 Contains

Id Name Short Name Type
IPR015590 Aldehyde dehydrogenase domain Aldehyde_DH_dom Domain
IPR002376 Formyl transferase, N-terminal Formyl_transf_N Domain
IPR009081 Acyl carrier protein-like Acyl_carrier_prot-like Domain
IPR016162 Aldehyde dehydrogenase N-terminal domain Ald_DH_N Domain
IPR016160 Aldehyde dehydrogenase, cysteine active site Ald_DH_CS_CYS Conserved_site
IPR001555 Phosphoribosylglycinamide formyltransferase, active site GART_AS Active_site
IPR005793 Formyl transferase, C-terminal Formyl_trans_C Domain

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Cook RJ Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. 1991 J Biol Chem 266 4965-73
Tsybovsky Y Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases. 2007 Biochemistry 46 2917-29
Donato H 10-formyltetrahydrofolate dehydrogenase requires a 4'-phosphopantetheine prosthetic group for catalysis. 2007 J Biol Chem 282 34159-66



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)