ID   IOLA1_BACLD             Reviewed;         484 AA.
AC   Q65IX1; Q62UD1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 133.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSDH 1 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA1 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   OrderedLocusNames=BLi02104, BL00293;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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}.
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DR   EMBL; CP000002; AAU23628.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40993.1; -; Genomic_DNA.
DR   RefSeq; WP_003182372.1; NC_006270.3.
DR   AlphaFoldDB; Q65IX1; -.
DR   SMR; Q65IX1; -.
DR   STRING; 279010.BL00293; -.
DR   GeneID; 92861305; -.
DR   KEGG; bld:BLi02104; -.
DR   KEGG; bli:BL00293; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000000606; 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..484
FT                   /note="Malonate-semialdehyde dehydrogenase 1"
FT                   /id="PRO_0000352329"
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         384
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ   SEQUENCE   484 AA;  52593 MW;  C82EA4B0C8E8C8CB CRC64;
     MITTNAKKMM NHIDGEWVNS LGAESEEVVN PANGNVIAYA PLSVRADVDR AVQAAKHAYQ
     TWSLVPVPNR ARLLYKYLQL LQEQKEQLAD IITTENGKTL KDARGEVQRG IEVVELATAT
     PTLMMGESLP AIAGGIDGSI WRYPLGVVAG ITPFNFPMMV PLWMFPLAIA CGNTFVLKPS
     ERTPILAGKL VELFYEAGFP KGVLNLVHGG KDVVNGILEN DDIKAVSFVG SEPVAKYVYQ
     TGTANGKRVQ ALAGAKNHAI VMPDCHLEKT VQGIIGAAFG SSGERCMACS VAAVVDDIAD
     DFMEMLVSET RKLKTGDGRS EDHFVGPLIR EVHKQRVLDY IDSGIKEGAA LAVDGRNPDV
     REGYFVGATI FDHVTPEMKI WQDEIFAPVL SVVRVQDLDE GIELANQSKF ANGAVIYTSS
     GKSAQQFRDK IDAGMIGVNV NVPAPMAFFS FAGNKASFYG DLGTNGKDGV QFYTRKKVVT
     ERWF
//