IOLA3_BACCZ
ID IOLA3_BACCZ Reviewed; 487 AA.
AC Q4V1F6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Malonate-semialdehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MSA dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01670};
DE AltName: Full=Methylmalonate-semialdehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MMSA dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MSDH 3 {ECO:0000255|HAMAP-Rule:MF_01670};
DE EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN Name=iolA3 {ECO:0000255|HAMAP-Rule:MF_01670};
GN OrderedLocusNames=pE33L466_0301;
OS Bacillus cereus (strain ZK / E33L).
OG Plasmid pE33L466.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
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}.
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; CP000040; AAY60451.1; -; Genomic_DNA.
DR RefSeq; WP_000218121.1; NZ_CP009967.1.
DR AlphaFoldDB; Q4V1F6; -.
DR SMR; Q4V1F6; -.
DR EnsemblBacteria; AAY60451; AAY60451; pE33L466_0301.
DR KEGG; bcz:pE33L466_0301; -.
DR PATRIC; fig|288681.22.peg.5505; -.
DR OMA; NWTLRQP; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000002612; Plasmid pE33L466.
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; Plasmid.
FT CHAIN 1..487
FT /note="Malonate-semialdehyde dehydrogenase 3"
FT /id="PRO_0000352324"
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 487 AA; 53055 MW; 478AEAC6D89DF5F9 CRC64;
MTVQTAQIVK NYIGGEWVES ISTKMEAVYN PATGEVIAQV PLSTKVDVEQ AVLAANEAFK
SWSKTAVPKR ARILFKYQQL LVDNWEDLAK LITIENGKSY NEAYGEVLRG IECVEFAAGA
PTLMMGKQLP DIATGIESGM YRYPIGVIGG ITPFNFPMMV PCWMFPLAIA CGNTFVLKPS
ERTPLLAAKL VELAEEAGLP KGVLNIVNGA HDVVNGLLEH KLVKAISFVG SQPVAEYVYK
KGTENLKRVQ ALAGAKNHSI VLSDANLELA TKQIISAAFG SAGERCMAAS VVTVQEEIAD
QLVGRLVEEA NKIVIGNGLD EDVFLGPVIR DNHKERTIGY IDSGVEQGAT LVRDGREDTA
VKGAGYFVGP TIFDHVTQEM KIWQDEIFAP VLSIVRVKSL DEAIEIANES RFANGACIYT
DSGASVRQFR ETIESGMLGV NVGVPAPMAF FPFSGWKDSF YGDLHANGTD GVEFYTRKKM
LTSRWEK
