IOLA_LACCA
ID IOLA_LACCA Reviewed; 492 AA.
AC A5YBJ3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Lactobacillus casei.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL23;
RX PubMed=17449687; DOI=10.1128/aem.00243-07;
RA Yebra M.J., Zuniga M., Beaufils S., Perez-Martinez G., Deutscher J.,
RA Monedero V.;
RT "Identification of a gene cluster allowing Lactobacillus casei BL23 the
RT utilization of myo-inositol.";
RL Appl. Environ. Microbiol. 73:3850-3858(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}.
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DR EMBL; EF382358; ABP57762.1; -; Genomic_DNA.
DR RefSeq; WP_003577405.1; NZ_MODT01000071.1.
DR AlphaFoldDB; A5YBJ3; -.
DR SMR; A5YBJ3; -.
DR STRING; 1582.AAW28_06915; -.
DR GeneID; 61268585; -.
DR eggNOG; COG1012; Bacteria.
DR OMA; VGAAKEW; -.
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..492
FT /note="Malonate-semialdehyde dehydrogenase"
FT /id="PRO_0000352344"
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 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ SEQUENCE 492 AA; 53716 MW; 276BA314BDA26D8F CRC64;
MDTTKQNVKT LKNFINGKWV DAKTETFENV YNPATGDVLA RVPHSTSEDV ADAVTAAKEA
FKIWQKVSIP KRAKILFKYQ QLLVEHQEEL GRIVTEENGK SLDEAVAEVG RGIENVEFAA
GVPTLMMGDS LSSVATDVEA TNYRYPIGVV GGITPFNFPM MVPCWMFPMA VATGNTFILK
PSEKTPLTSQ RLVELFQEAG LPDGVLNIVN GAVDVVNGIL DHPDIKAISF VGSERVGEYV
YKRGSDHLKR VQALTGAKNH TIVLADADLD AAVKGIISSS FGSAGERCMA TSVLVLQDEI
ADKFMAKFTQ AAKDIKIGNG LDKGVFLGPV IRKENQERTL NYIQTGVKEG AKLVLDGSAE
AKKHDGYFVG PTIFEDVKTD MTIWHDEMFA PVLSVIRAKD LPQAVAIANT SELANGACLF
TDSAASIRYF RENIDAGMLG INLGVPAPIA VFPFSGWKHS FFGTLHANGK DSVDFYTHKK
VVTARYDQRR FK
