ID IOLA_BACVZ Reviewed; 487 AA. AC A7ZAI1; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=Malonate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670}; DE EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670}; DE AltName: Full=Methylmalonate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MMSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670}; DE Short=MSDH {ECO:0000255|HAMAP-Rule:MF_01670}; GN Name=iolA {ECO:0000255|HAMAP-Rule:MF_01670}; GN OrderedLocusNames=RBAM_036780; OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) OS (Bacillus amyloliquefaciens subsp. plantarum). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus amyloliquefaciens group. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant growth- RT promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). 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 --------------------------------------------------------------------------- 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; CP000560; ABS76007.1; -; Genomic_DNA. DR RefSeq; WP_012118848.1; NC_009725.2. DR AlphaFoldDB; A7ZAI1; -. DR SMR; A7ZAI1; -. DR GeneID; 93082817; -. DR KEGG; bay:RBAM_036780; -. DR HOGENOM; CLU_005391_1_10_9; -. DR UniPathway; UPA00076; UER00148. DR Proteomes; UP000001120; Chromosome. 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; Reference proteome. FT CHAIN 1..487 FT /note="Malonate-semialdehyde dehydrogenase" FT /id="PRO_0000352317" FT ACT_SITE 284 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" 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 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 382 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" SQ SEQUENCE 487 AA; 53529 MW; CB86A763E9D08C6F CRC64; MAEIRKLKNY INGEWVESKT DQYEDVINPA TKEVMCQVPI STREDVEYAV RSASEAFQTW SKTAVPRRAR ILFNYQQLLQ QNKEELARLI TLENGKNTTE ALGEVGRGIE NVEFAAGAPS LMMGDSLASI ATDVEAANYR YPIGVVGGIA PFNFPMMVPC WMFPMAISLG NTFILKPSER TPLLTEKLAE LFEQAGLPKG VFNVVHGAHD VVNGVLEHPD IKAISFVGSK PVGEYVFKKG SEHLKRVQAL TGAKNHTIVL NDAHLEDTVT NIIGAAFGSA GERCMACAVV TVEEGIADEF MAKLQEKAAD IKIGNGLDDG VFLGPVIRED NKKRTHSYIE KGIEEGARLL CDGRENATED GYFVGPTIFD NVTTDMTIWK DEIFAPVLSV IRVKNLKEAV DIANQSEFAN GACLFTSNAN AIRYFRENID AGMLGINLGV PAPMAFFPFS GWKSSFFGTL HANGKDSVDF YTRKKVVTAR YPSPDFN //