IOLA_LISMC
ID IOLA_LISMC Reviewed; 488 AA.
AC C1KZ99;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Lm4b_00401;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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; FM242711; CAS04169.1; -; Genomic_DNA.
DR RefSeq; WP_003728135.1; NC_012488.1.
DR AlphaFoldDB; C1KZ99; -.
DR SMR; C1KZ99; -.
DR KEGG; lmc:Lm4b_00401; -.
DR HOGENOM; CLU_005391_1_10_9; -.
DR OMA; VGAAKEW; -.
DR BioCyc; LMON568819:LM4B_RS01995-MON; -.
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..488
FT /note="Malonate-semialdehyde dehydrogenase"
FT /id="PRO_1000215882"
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 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ SEQUENCE 488 AA; 53290 MW; B23436CBA9108A4C CRC64;
MADVRKLKNY INGEWVESRA DKYEDVINPA TGEVLCQVPI STRAELDQAA VIAEQAFEKW
SQVAVPRRAR VLFSFQQLLI QHKEELARLI TLENGKNLSE ARGEVQRGIE NVEFAAGAPT
LMMGDSLASI ATDVEAANYR YPVGVVGGIA PFNFPMMVPC WMFPMAIALG NSFILKPSER
TPLLMEKLVE LFSEAGLPKG VFNVVYGAHD VVNGILENEI IKAVSFVGSK PVGEYVYKTG
SANLKRVQAL TGAKNHTIVL NDADLEDTVT NVISAAFGSA GERCMACAVV TVEEGIADEF
LAALRTAAQN VKIGNGLDDG VFLGPVIREE NQKRTIAYIE KGLEEGAKLT VDGRETGLSE
GHFVGPTILE DVTTDMTIWK DEIFAPVLSV IRVKNLQEAV RVANQSEFAN GACIFTNNAK
AIRYFREKID AGMLGVNLGV PAPMAFFPFS GWKSSFYGTL HANGKDSVDF YTHKKVVTAR
YSLKGYEE
