IOLA_LISIN
ID IOLA_LISIN Reviewed; 488 AA.
AC Q92EQ7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=lin0401;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596164; CAC95634.1; -; Genomic_DNA.
DR PIR; AB1483; AB1483.
DR RefSeq; WP_010990384.1; NC_003212.1.
DR AlphaFoldDB; Q92EQ7; -.
DR SMR; Q92EQ7; -.
DR STRING; 272626.lin0401; -.
DR EnsemblBacteria; CAC95634; CAC95634; CAC95634.
DR KEGG; lin:lin0401; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_10_9; -.
DR OMA; VGAAKEW; -.
DR OrthoDB; 490746at2; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000002513; 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..488
FT /note="Malonate-semialdehyde dehydrogenase"
FT /id="PRO_0000352345"
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; 53248 MW; 787B0C3D6EC7026C CRC64;
MADVRKLKNY INGEWVESKA DKYEDVINPA TGEVLCQVPI STRAELDQAA VIAEQAFEKW
SQVAVPRRAR VLFSFQQLLI QHKEELARLI TLENGKNLSE ARGEVQRGIE NVEFAAGAPT
LMMGDSLASI ATDVEAANYR YPVGVVGGIA PFNFPMMVPC WMFPMAIALG NSFILKPSER
TPLLMEKLVE LFSEAGLPKG VFNVVYGAHD VVNGILENET IKAVSFVGSK PVGEYVYKTG
SANLKRVQAL TGAKNHTIVL NDADLEDTVT NVISAAFGSA GERCMACAVV TVEEGIADDF
LAALRTAAQN VKIGNGLDDG VFLGPVIREE NQKRTIAYIE KGVEEGAKLT VDGRETGLSE
GYFVGPTILE DVTTDMTIWK DEIFAPVLSV IRVKNLQEAV RVANQSEFAN GACIFTNNAK
AIRYFREKID AGMLGVNLGV PAPMAFFPFS GWKSSFYGTL HANGKDSVDF YTHKKVVTAR
YSLKGYEE
