ID   IOLA3_GEOKA             Reviewed;         484 AA.
AC   Q5KYK0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate-semialdehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSDH 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA3 {ECO:0000255|HAMAP-Rule:MF_01670}; OrderedLocusNames=GK1951;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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=BAD76236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000043; BAD76236.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5KYK0; -.
DR   SMR; Q5KYK0; -.
DR   STRING; 235909.GK1951; -.
DR   EnsemblBacteria; BAD76236; BAD76236; GK1951.
DR   KEGG; gka:GK1951; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000001172; 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..484
FT                   /note="Malonate-semialdehyde dehydrogenase 3"
FT                   /id="PRO_0000352341"
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         384
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ   SEQUENCE   484 AA;  52987 MW;  705FF4F4AC4BB3B6 CRC64;
     MTETKTLKNF IGGQWVASTS GKEEVVPNPA TGEVLAKVPL SSREELDAAV AAAKEAFREW
     RKVPVPRRAR ILFRYQQLLV EHWDELARLV TLENGKVYED AYGEVQRGIE CVEFAAGIPT
     LMMGQQLPDI ATDIESGMYR YPLGVVAGIT PFNFPMMVPC WMFPLAIACG NTFVLKPSER
     TPMLANRLAE LFTEAGLPPG VLNIVHGAHE VVGGILEHKD IKAVSFVGSQ PVAEYVYKTA
     AAHGKRVQAL AGAKNHSIVM PDADLDMAVT NIINAAFGSA GERCMACSVV VAVGDIADEL
     VRRLKEAADR IQIGNGLDKG VFLGPVIRES HKERTIKYIE IGEKEGALLV RDGRRDSATS
     GQGYFIGPTI FDHVKPGMTI WTDEIFAPVL SVVRARDLDE AIEIANRSEF ANGACIYTDS
     AKAIRQFREE IDAGMLGVNV AVPAPMAFFP FSGYKNSFYG DLHANGRDGV EFYTRKKMVT
     ARYQ