InterPro : IPR010061

Name  Methylmalonate-semialdehyde dehydrogenase Short Name  MeMal-semiAld_DH
Type  Family Description  Methylmalonate-semialdehyde dehydrogenase catalyses the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterised in both prokaryotes [, ]and eukaryotes [], functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in Pseudomonas aeruginosadoes not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase []. In most cases these enzymes are involved in valine metabolism, but Gram-positive bacteria, such as Bacillus, contain a distinct subset. This subset of enzymes is encoded in an iol operon and is apparently involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2 [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR023510 Methylmalonate-semialdehyde dehydrogenase, Gram-positive bacteria MeMal-semiAld_DH_GmP_bac Family

2 Contains

Id Name Short Name Type
IPR015590 Aldehyde dehydrogenase domain Aldehyde_DH_dom Domain
IPR016162 Aldehyde dehydrogenase N-terminal domain Ald_DH_N Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Steele MI Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. 1992 J Biol Chem 267 13585-92
Zhang YX Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor. 1996 J Bacteriol 178 490-5
Kedishvili NY CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. 1992 J Biol Chem 267 19724-9
Yoshida KI Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis. 1997 J Bacteriol 179 4591-8

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)