ID   IOLA1_ALKCK             Reviewed;         491 AA.
AC   Q5WKZ1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=ABC0422;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP006627; BAD62964.1; -; Genomic_DNA.
DR   RefSeq; WP_011245283.1; NC_006582.1.
DR   AlphaFoldDB; Q5WKZ1; -.
DR   SMR; Q5WKZ1; -.
DR   STRING; 66692.ABC0422; -.
DR   EnsemblBacteria; BAD62964; BAD62964; ABC0422.
DR   KEGG; bcl:ABC0422; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   OMA; VGAAKEW; -.
DR   OrthoDB; 490746at2; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000001168; 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..491
FT                   /note="Malonate-semialdehyde dehydrogenase 1"
FT                   /id="PRO_0000352326"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT   BINDING         180..184
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   491 AA;  53477 MW;  D12D2FFD4698A92B CRC64;
     MGETTVEVRK VKNYINGKWI ESSTSLYEDV VNPATKEVIC QVPLSTKADV EYAVEAAKTA
     FAKWSKVAVP RRARILFNYQ QLLQRDKEEL ARLITIENGK NLTEARGEVQ RGIENVEFAA
     GAPSLMMGDS LPMIATDVEA SNYRYPIGVV GGIAPFNFPM MVPCWMFPMA IALGNAFLLK
     PSERTPLLTE KLADLLTEAG VPDGVFNVVY GAHDVVNGML EHPDIKAISF VGSKPVGEYV
     YKKASENLKR VQALTGAKNH TIVLNDADLD DAVTNIAGAA FGSAGERCMA CAVVTVEEGI
     ADAFVAKLKA KAESLVMGNG LDDGVFLGPV IREENKNRTI AYIEKGVEEG ATLVCDGRSR
     VSADGYFIGP TIFENVTTDM TIWKDEIFAP VLSIIRVKNL DEGIQIANRS EFANGACLFT
     TNAAAVRYFR ENIDAGMLGI NLGVPAPMAF FPFSGWKSSF YGTLHANGKD SVDFYTRKKV
     VTARYPKPSF D