IOLA_ALKHC
ID IOLA_ALKHC Reviewed; 485 AA.
AC Q9KAH5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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}; OrderedLocusNames=BH2312;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000004; BAB06031.1; -; Genomic_DNA.
DR PIR; H83938; H83938.
DR RefSeq; WP_010898468.1; NC_002570.2.
DR AlphaFoldDB; Q9KAH5; -.
DR SMR; Q9KAH5; -.
DR STRING; 272558.10174932; -.
DR PRIDE; Q9KAH5; -.
DR EnsemblBacteria; BAB06031; BAB06031; BAB06031.
DR KEGG; bha:BH2312; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_9; -.
DR OMA; HGKRAQC; -.
DR OrthoDB; 490746at2; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000001258; 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..485
FT /note="Malonate-semialdehyde dehydrogenase"
FT /id="PRO_0000352328"
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 179..183
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 485 AA; 52936 MW; 62874DF9CB328A5D CRC64;
MANLATGEKL KNFIGGQWVE SDSGKTEAVP NPATGEILAH VPISNREDLD RAVSVAKEAF
KTWGKTPVPR RARVLFKYQQ LLVENWEELA RLVTLENGKS YKEAYGEVQR GIECVEFAAG
APSLMMGKQL PDIATNIESG MYRYPIGVVG GITPFNFPMM VPCWMFPLAI ACGNTFVLKP
SERTPLLANR LAELFTEAGL PEGVLNIVHG AHDVVNGLLE HPDVKAISFV GSQPVAEYVY
KTASQHGKRV QALAGAKNHS IVMPDADLDG AVNQIVNAAY GSAGERCMAA AVVVAVGEVA
EPLMEKLQKA VNEITIGNGL DDDVFLGPVI RESHKQKTEN YIELGEKEGA TLVRDGRKDN
VSKDGYFLGP TLFDNVTTEM TIWKEEIFAP VLSVVRVESL DEAIQLTNQS EFANGACLYT
TNGSSVRKFR EEIDAGMLGI NLGVPAPMAF FPFSGWKNSF YGDLHANGTD GVEFYTRKKM
ITARW
