AC MF_01670; DC Protein; auto TR HAMAP; MF_01670; -; 1; level=0 XX Names: IolA XX ID IOLA DE RecName: Full=Malonate-semialdehyde dehydrogenase; DE Short=MSA dehydrogenase; DE EC=1.2.1.27; DE AltName: Full=Methylmalonate semialdehyde dehydrogenase; DE Short=MMSA dehydrogenase; DE Short=MSDH; GN Name=iolA; XX CC -!- FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and CC methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, CC respectively. Is involved in a myo-inositol catabolic pathway. CC Bicarbonate, and not CO2, is the end-product of the enzymatic reaction. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxopropanoate + CoA + H2O + NAD(+) = acetyl-CoA + H(+) + CC hydrogencarbonate + NADH; Xref=Rhea:RHEA:76615, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:33190, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.27; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76616; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20805; CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA; CC acetyl-CoA from myo-inositol: step 7/7. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA CC subfamily. XX DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1; trigger=no DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1; trigger=no DR Pfam; PF00171; Aldedh; 1; trigger=no DR NCBIfam; TIGR01722; MMSDH; 1; trigger=no XX KW NAD KW Oxidoreductase XX GO GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity GO GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity GO GO:0019310; P:inositol catabolic process XX FT From: IOLA_BACSU (P42412) FT BINDING 150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: A FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: F FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: K FT BINDING 179 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: E FT BINDING 180 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [KR] FT BINDING 229 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: T FT BINDING 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: T FT BINDING 382 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: E FT ACT_SITE 284 FT /note="Nucleophile" XX Size: 470-520; Related: None; Template: P42412; Scope: Bacteria; Bacillota Fusion: Nter: None Cter: None Duplicate: in BACAH, BACAN, BACCZ, BACHK, BACLD, SHOC1, BACMK, GEOKA, GEOTN, OCEIH Plasmid: in BACCZ Comments: None XX # Revision 1.17 2023/11/28 //