ID IOLA2_BACAN Reviewed; 487 AA.
AC Q81QB6; Q6HYJ3; Q6KSJ4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Malonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
DE AltName: Full=Methylmalonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MMSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE Short=MSDH 2 {ECO:0000255|HAMAP-Rule:MF_01670};
GN Name=iolA2 {ECO:0000255|HAMAP-Rule:MF_01670};
GN OrderedLocusNames=BA_2513, GBAA_2513, BAS2334;
OS Bacillus anthracis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
CC -!- FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and
CC methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA,
CC respectively. Is involved in a myo-inositol catabolic pathway.
CC Bicarbonate, and not CO2, is the end-product of the enzymatic reaction.
CC {ECO:0000255|HAMAP-Rule:MF_01670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + H2O + NAD(+) = acetyl-CoA + H(+) +
CC hydrogencarbonate + NADH; Xref=Rhea:RHEA:76615, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.27; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76616;
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20805;
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; AE016879; AAP26371.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31624.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54646.1; -; Genomic_DNA.
DR RefSeq; NP_844885.1; NC_003997.3.
DR RefSeq; WP_000218128.1; NZ_WXXJ01000008.1.
DR RefSeq; YP_028595.1; NC_005945.1.
DR AlphaFoldDB; Q81QB6; -.
DR SMR; Q81QB6; -.
DR IntAct; Q81QB6; 7.
DR STRING; 261594.GBAA_2513; -.
DR DNASU; 1084066; -.
DR GeneID; 45022376; -.
DR KEGG; ban:BA_2513; -.
DR KEGG; bar:GBAA_2513; -.
DR KEGG; bat:BAS2334; -.
DR PATRIC; fig|198094.11.peg.2485; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_9; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07085; ALDH_F6_MMSDH; 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 NCBIfam; TIGR01722; MMSDH; 1.
DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43866:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..487
FT /note="Malonate-semialdehyde dehydrogenase 2"
FT /id="PRO_0000352319"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 231
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; 53139 MW; EB15A1E2ED983F76 CRC64;
MTVQTAQIVK NYIGGEWVES ISTKMEAVYN PATGEVIAQV PLSTKVDVEQ AVLAANEAFK
SWSKTAVPRR ARILFKYQQL LVDNWEELAK LITIENGKSY NEAYGEVLRG IECVEFAAGA
PTLMMGKQLP DIATGIESGM YRYPIGVIGG ITPFNFPMMV PCWMFPLAIA CGNTFVLKPS
ERTPLLAARL AELAEEAGLP KGVLNIVNGA HDVVNGLLEH KLVKAISFVG SQPVAEYVYK
KGTENLKRVQ ALAGAKNHSI VLNDANLELA TKQIISAAFG SAGERCMAAS VVTVEEEIAD
QLVERLVAEA NKIVIGNGLD EDVFLGPVIR DNHKERTIGY IDSGVEQGAT LVRDGREDTA
VKGAGYFVGP TIFDHVTKEM KIWQDEIFAP VLSIVRVKSL DEAIEIANES RFANGACIYT
DSGASVRQFR ETIESGMLGV NVGVPAPMAF FPFSGWKDSF YGDLHANGTD GVEFYTRKKM
LTSRWEK
//
