ID IOLA2_BACMK Reviewed; 483 AA. AC A9VMS6; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 2. DT 04-NOV-2026, entry version 97. DE RecName: Full=Malonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670}; DE EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670}; DE AltName: Full=Methylmalonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MMSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MSDH 2 {ECO:0000255|HAMAP-Rule:MF_01670}; GN Name=iolA2 {ECO:0000255|HAMAP-Rule:MF_01670}; GN OrderedLocusNames=BcerKBAB4_3173; OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). 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 {ECO:0000255|HAMAP-Rule:MF_01670}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxopropanoate + NAD(+) + CoA + H2O = hydrogencarbonate + CC acetyl-CoA + NADH + H(+); 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01670}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76616; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01670}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-methyl-3-oxopropanoate + NAD(+) + CoA + H2O = propanoyl-CoA CC + hydrogencarbonate + NADH + H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_01670}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20805; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01670}; CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA; CC acetyl-CoA from myo-inositol: step 7/7. {ECO:0000255|HAMAP- CC Rule:MF_01670}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01670}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01670}. CC -!- SEQUENCE CAUTION: CC Sequence=ABY44349.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000903; ABY44349.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; A9VMS6; -. DR SMR; A9VMS6; -. DR KEGG; bwe:BcerKBAB4_3173; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_0_9; -. DR OMA; AAAFPMW; -. DR UniPathway; UPA00076; UER00148. DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule. DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-UniRule. DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006574; P:L-valine catabolic process; IEA:TreeGrafter. DR GO; GO:0006210; P:thymine catabolic process; IEA:TreeGrafter. DR CDD; cd07085; ALDH_F6_MMSDH; 1. DR FunFam; 3.40.309.10:FF:000002; Methylmalonate-semialdehyde dehydrogenase (Acylating); 1. DR FunFam; 3.40.605.10:FF:000003; Methylmalonate-semialdehyde dehydrogenase [acylating]; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR HAMAP; MF_01670; IolA; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR010061; MeMal-semiAld_DH. DR InterPro; IPR023510; MSDH_GmP_bac. DR NCBIfam; TIGR01722; MMSDH; 1. DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43866:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT CHAIN 1..483 FT /note="Malonate-semialdehyde dehydrogenase 2" FT /id="PRO_0000352338" FT ACT_SITE 284 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 179 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 180 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 229 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 384 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" SQ SEQUENCE 483 AA; 52736 MW; 41598A0DA018827A CRC64; MKNVQTLKNY IGGQWIESTS KQVEDVPNPA TGEIIARVPL STKEDLDRAV ATAKEAFKTW RKVAVPRRAR ILFRYQQLLI ENWEGLAKLV TLENGKSYKE AYGEVQRGIE CVEFAAGAPT LMMGEQLPDI ATGVESGMYR YPIGVIAGIT PFNFPMMVPC WMFPLAIACG NTFVLKPSER TPLLANRIAE LFKEAGLPDG VLNIVHGAHD VVNGILDNED VKAVSFVGSQ PVAEYIYKTA AANGKRVQAL AGAKNHSIVL KDADLSSTVK EITSAAFGSA GERCMAAAVV VVEEDVADEL VNRLLQEANA ITIGNGLEEG VFLGPVIREG HKERTLGYIQ SGVEQGATLI RDGREDDIAN SQGYFVGPTI FDNVTQEMKI WQDEIFAPVL SIVRVKDLME AIHVANASPF ANGACLYTNS AKAIREFREE IDAGMLGVNL GVPAPMAFFP FSGYKKSFYG DLHANGKDGV EFYTRKKMLT ARY //