ID IOLA_BACP2 Reviewed; 486 AA. AC A8FDV4; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 110. 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=BPUM_1749; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(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; CP000813; ABV62421.1; -; Genomic_DNA. DR RefSeq; WP_012010148.1; NC_009848.4. DR AlphaFoldDB; A8FDV4; -. DR SMR; A8FDV4; -. DR STRING; 315750.BPUM_1749; -. DR PaxDb; 315750-BPUM_1749; -. DR GeneID; 5621010; -. DR KEGG; bpu:BPUM_1749; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_0_9; -. DR OrthoDB; 9762913at2; -. DR UniPathway; UPA00076; UER00148. DR Proteomes; UP000001355; 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..486 FT /note="Malonate-semialdehyde dehydrogenase" FT /id="PRO_0000352331" FT ACT_SITE 286 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 154 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 178 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 181 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 182 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 231 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" FT BINDING 386 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670" SQ SEQUENCE 486 AA; 53208 MW; 418DF7891FAED79E CRC64; MTKTDVQMLK NYIGGQWIEA ETSQTEAVYN PATGKIIAEV PLSTKKDVER AVQAAQEAFT TWSKTPVPRR ARILFKYQQL LVDKWDELAE LVTMENGKSI TEAKGEVQRG IECVEFAAGA PTLMMGKQLP DIASGLESGM YRYPIGVIGG ITPFNFPMMV PCWMFPLAIA CGNTFVLKPS ERTPILAARL AELFEEAGLP KGVLNIVNGA HDVVNGLLEH QKVKAISFVG SQPVAEYVYK KGTEHGKRVQ ALAGAKNHSI VLKDADLDAA TKQIIGAAFG SAGERCMAAA VVAVEEEVAD DLIQKLVDES NELVIGNGIN EEVFLGPVIR EEHKERTLQY IQSGIEEGAS LIRDGRKDHE TNGKGYFVGP TIFDHVTNQM KIWQDEIFAP VLSIVRVSSL AEAIDLSNQS KFANGACLYT DSASSIREFR ENIEAGMLGV NIGVPAPMAF FPFSGWKDSF YGDLHANGTD GVEFYTRKKM VTARYM //