ID IOLA2_GEOKA Reviewed; 484 AA.
AC Q5KYR4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 102.
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}; OrderedLocusNames=GK1887;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD76172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000043; BAD76172.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5KYR4; -.
DR SMR; Q5KYR4; -.
DR STRING; 235909.GK1887; -.
DR KEGG; gka:GK1887; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_9; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000001172; 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..484
FT /note="Malonate-semialdehyde dehydrogenase 2"
FT /id="PRO_0000352340"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 180
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 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT BINDING 385
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ SEQUENCE 484 AA; 53035 MW; 77C7333D2B9EF600 CRC64;
MTTGVQTLKN YIGGQWVESR SGKTEAVPNP ATGEVLAYVP ISSREELDEA VRAAKEAFKT
WRKTPVPRRA RILFKYQQLL VEHWEELARL VTLENGKSYN EAYGEVQRGI ECVEFAAGAP
TLMMGRQLPD IATGIESGMY RYPIGVVGGI TPFNFPMMVP CWMFPLAIAC GNTFVLKPSE
RTPMLANRLA ELFKEAGLPD GVLNIVHGAH DVVNGLLEHP DVKAISFVGS QPVGEYVYKT
AAAHGKRVQA LTGAKNHSIV MPDADLNVAV REIINAAFGS AGERCMAASV VVAVGEIADE
LVEKLVAAAN ELKIGNGLEE SVFLGPVIRE AHKQRTVKYI ELGEKEGAIL VRDGRKDAAV
QDNGYFIGPT IFDRVTTDMT IWKDEIFAPV LSIVRVETLD EAIEVANKSP FANGACIYTR
DGGNVRKFRE EIDAGMLGVN LGVPAPMAFF PFSGWKNSFY GDLHANGMDG VEFYTRKKMM
TSRW
//
