IOLA1_BACHK
ID IOLA1_BACHK Reviewed; 486 AA.
AC Q6HJ19;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=BT9727_2130;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT59833.1; -; Genomic_DNA.
DR RefSeq; WP_000633351.1; NC_005957.1.
DR RefSeq; YP_036457.1; NC_005957.1.
DR AlphaFoldDB; Q6HJ19; -.
DR SMR; Q6HJ19; -.
DR EnsemblBacteria; AAT59833; AAT59833; BT9727_2130.
DR GeneID; 56652101; -.
DR KEGG; btk:BT9727_2130; -.
DR PATRIC; fig|281309.8.peg.2242; -.
DR HOGENOM; CLU_005391_1_10_9; -.
DR OMA; HIYGNDG; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000001301; 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.
FT CHAIN 1..486
FT /note="Malonate-semialdehyde dehydrogenase 1"
FT /id="PRO_0000352335"
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; 52975 MW; 22F24884D36498B3 CRC64;
MITTEIKRVK NHINGEWVES TGTEVEAVPN PATGKIIAYV PLSPKEDVEK AVEAAKAAYE
TWSKVPVPNR SRQLYKYLQL LQENKEELAK IITLENGKTL TDATGEVQRG IEAVELATSA
PNLMMGQALP NIASGIDGSI WRYPIGVVAG ITPFNFPMMI PLWMFPLAIA CGNTFVLKTS
ERTPLLAERL VELFYEAGFP KGVLNLVQGG KDVVNSILEN KDIQAVSFVG SEPVARYVYE
TGTKHGKRVQ ALAGAKNHAI VMPDCNLEKT VQGVIGSAFA SSGERCMACS VVAVVDEIAD
EFIDVLVAET KKLKVGDGFH EDNYVGPLIR ESHKERVLGY INSGVADGAT LLVDGRKIKE
EVGEGYFVGA TIFDGVNQEM KIWQDEIFAP VLSIVRVKDL EEGIKLTNQS KFANGAVIYT
SNGKHAQTFR DNIDAGMIGV NVNVPAPMAF FAFAGNKASF FGDLGTNGTD GVQFYTRKKV
VTERWF
