HMM Summary Page: TIGR01722

AccessionTIGR01722
NameMMSDH
Functionmethylmalonate-semialdehyde dehydrogenase (acylating)
Gene SymbolmmsA
Trusted Cutoff448.50
Domain Trusted Cutoff448.50
Noise Cutoff392.40
Domain Noise Cutoff392.40
Isology Typeequivalog
EC Number1.2.1.27
HMM Length477
Mainrole CategoryEnergy metabolism
Subrole CategoryAmino acids and amines
Gene Ontology TermGO:0004491: methylmalonate-semialdehyde dehydrogenase (acylating) activity molecular_function
GO:0006574: valine catabolic process biological_process
AuthorBrinkac L
Entry DateOct 10 2002 2:02PM
Last ModifiedFeb 14 2011 3:27PM
CommentInvolved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA [1]. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes [1,2] and eukaryotes [3], functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver [1]. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (PF00171), 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 [3]. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2 [4]. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus.
ReferencesRN [1] RM 1339433 RT Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. RA Steele MI, Lorenz D, Hatter K, Park A, Sokatch JR. RL J Biol Chem. 1992 Jul 5;267(19):13585-92. RN [2] RM 8550471 RT Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor. RA Zhang YX, Tang L, Hutchinson CR. RL J Bacteriol. 1996 Jan;178(2):490-5. RN [3] RM 1527093 RT CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. RA Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA. RL J Biol Chem. 1992 Sep 25;267(27):19724-9 RN [4] RM 9226270 RT Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis. RA Yoshida KI, Aoyama D, Ishio I, Shibayama T, Fujita Y. RL J Bacteriol. 1997 Jul;179(14):4591-8. DR PFAM; PF00171; Aldehyde dehydrogenase family DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS DR EXPERIMENTAL; SP|P28810; Pseudomonas aeruginosa; characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. DR EXPERIMENTAL; SP|Q07536; Bos taurus; novel use of an iodo-myristyl-CoA analog identifies a semialdehyde dehydrogenase in bovine liver DR EXPERIMENTAL; GP|1041092; Streptomyces coelicolor; cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces DR OUTGROUP; SP|P17445; Escherichia coli; Betaine aldehyde dehydrogenase DR HAMAP; MF_01670; 34 of 34
Genome PropertyGenProp1071: myo-inositol catabolism (HMM)