ID   IOLA1_OCEIH             Reviewed;         486 AA.
AC   Q8ES27;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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.- {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};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA1 {ECO:0000255|HAMAP-Rule:MF_01670}; OrderedLocusNames=OB0816;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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   ---------------------------------------------------------------------------
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; BA000028; BAC12772.1; -; Genomic_DNA.
DR   RefSeq; WP_011065222.1; NC_004193.1.
DR   AlphaFoldDB; Q8ES27; -.
DR   SMR; Q8ES27; -.
DR   STRING; 221109.22776496; -.
DR   EnsemblBacteria; BAC12772; BAC12772; BAC12772.
DR   KEGG; oih:OB0816; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   OMA; HIYGNDG; -.
DR   OrthoDB; 490746at2; -.
DR   PhylomeDB; Q8ES27; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000000822; Chromosome.
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; Reference proteome.
FT   CHAIN           1..486
FT                   /note="Malonate-semialdehyde dehydrogenase 1"
FT                   /id="PRO_0000352348"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT   BINDING         178..182
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;  53305 MW;  DDDFD9039035CE61 CRC64;
     MISSETKHMQ NYINGKWVDA KSGKQEVIPN PATGETIATV TISDVEDVDM AVAAAKEVFP
     EWSDIPVPNR TRYLLDYWKL LQDNKEELAK IITLENGKSL RDAQGEVQRG IEVVELATST
     PSMMMGDALP SIAKGIDGSI WRYPLGVVAG ITPFNFPMMV PLWMFPLAIA CGNTFVLKTS
     ERTPILAERL VELFYEAGFP KGVLNLVHGG KEVVNRFLTH PDIEAVSFVG SEPVAKHVYQ
     TGTAHGKRVQ ALAGAKNHAV VMPDCDVEKT IQGVLGAAFG SSGERCMACS VVAVVDDIAD
     EFLEKLVKET KKLRVGDGMD DSNFIGPVIR ESHKERVLSY IDSGVDEGAH LLVDGRKIKE
     ETPDGYYVGA TIFDHVTQDM KIWQDEIFAP VLSVVRVSDL EEGIRVTNQS KFANGAVIYT
     NSGKSAQQFR NRIDAGMIGV NVNVPAPMAF FSFAGNKASF YGDLGTNGKD GVQFYTRKKV
     VTERWF