ID   IOLA_BACNA              Reviewed;         487 AA.
AC   A7BJC4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 56.
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.- {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};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA {ECO:0000255|HAMAP-Rule:MF_01670};
OS   Bacillus subtilis subsp. natto.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Miyagino;
RX   PubMed=17928718; DOI=10.1271/bbb.70223;
RA   Kimura K., Itoh Y.;
RT   "Determination and characterization of IS4Bsu1-insertion loci and
RT   identification of a new insertion sequence element of the IS256 family in a
RT   natto starter.";
RL   Biosci. Biotechnol. Biochem. 71:2458-2464(2007).
CC   -!- FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and
CC       methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA,
CC       respectively. {ECO:0000255|HAMAP-Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC         Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01670};
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         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=BAF74776.1; 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; AB304464; BAF74776.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014481419.1; NZ_SJSU01000040.1.
DR   AlphaFoldDB; A7BJC4; -.
DR   SMR; A7BJC4; -.
DR   UniPathway; UPA00076; UER00148.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   PANTHER; PTHR43866; PTHR43866; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..487
FT                   /note="Malonate-semialdehyde dehydrogenase"
FT                   /id="PRO_0000352332"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT   BINDING         176..180
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;  53461 MW;  ABB479387DF2B49C CRC64;
     MAEIRKLKNY INGEWVESKT DQYEDVVNPA TKEVLCQVPI STKEDIDYAA QTAAEAFETW
     SKVAVPRRAR ILFNFQQLLS QHKEELAHLI TIENGKNTKE ALGEVGRGIE NVEFAAGAPS
     LMMGDSLASI ATDVEAANYR YPIGVVGGIA PFNFPMMVPC WMFPMAIALG NTFILKPSER
     TPLLTEKLVE LFEKAGLPKG VFNVVYGAHD VVNGILEHPE IKAISFVGSK PVGEYVYKKG
     SEHLKRVQSL TGAKNHTIVL NDANLEDTVT NIVGAAFGSA GERCMACAVV TVEEGIADEF
     MAKLQEKVAD IKIGNGLDDG VFLGPVIRED NKKRTLSYIE KGLEEGARLV CDGRENVSDD
     GYFVGPTIFD NVTTEMTIWK DEIFAPVLSV IRVKNLKEAI EIANKSEFAN GACLFTSNSN
     AIRYFRENID AGMLGINLGV PAPMAFFPFS GWKSSFFGTL HANGKDSVDF YTRKKVVTAR
     FPAPDFN