ID   IOLA2_OCEIH             Reviewed;         486 AA.
AC   Q8EMV4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSDH 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA2 {ECO:0000255|HAMAP-Rule:MF_01670}; OrderedLocusNames=OB2736;
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}.
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DR   EMBL; BA000028; BAC14692.1; -; Genomic_DNA.
DR   RefSeq; WP_011067130.1; NC_004193.1.
DR   AlphaFoldDB; Q8EMV4; -.
DR   SMR; Q8EMV4; -.
DR   STRING; 221109.22778423; -.
DR   EnsemblBacteria; BAC14692; BAC14692; BAC14692.
DR   KEGG; oih:OB2736; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   OMA; HGKRAQC; -.
DR   OrthoDB; 490746at2; -.
DR   PhylomeDB; Q8EMV4; -.
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 2"
FT                   /id="PRO_0000352349"
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;  53503 MW;  9C50FC90021C4E4A CRC64;
     MTQTTVKNVK NYIGGEWIES RTEKTEDVFN PATGEVIAQV PISTTEDVHH AIEVANEAFK
     TWKEVPVPKR ARILFKYQQL LVEHWEELAK LITLENGKNY AEAYGEVQRG IENVEFATGA
     PSLMMGEQLA SIATELESGV YRYPIGVIGG ITPFNFPMMV PCWMFPMAIA TGNTFVMKPS
     ERTPLLANRL AELLEEAGLP NGVFNIVHGA HDVVNGLLDH KKVAAISFVG SQPVAEYVYK
     RGTQNLKRVQ ALAGAKNHSI VLSDANLENA TTQILNAAFG SAGERCMAAS VVAVEEDVAD
     EFVTLLTQKA NEIKIGNGLD EGVFLGPVIR DQHKERTLQY IESGEEEGAN LVRDGRTDEA
     AKQEGYFVGP TIFDHVTSEM KIWQDEIFAP VLSIARVNNL EEGVDLANES RFANGACIFT
     RDGGSVRRFR ETIDAGMLGV NIGVPAPMAF LPFSGWKDSF YGDLHANGKD GLQFYTRKKV
     LTTKWV