ID A0A345PKG6_9BACI Unreviewed; 491 AA.
AC A0A345PKG6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Malonate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE Short=MSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE EC=1.2.1.27 {ECO:0000256|HAMAP-Rule:MF_01670};
DE AltName: Full=Methylmalonate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE Short=MMSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE Short=MSDH {ECO:0000256|HAMAP-Rule:MF_01670};
GN Name=mmsA {ECO:0000313|EMBL:AXI10496.1};
GN Synonyms=iolA {ECO:0000256|HAMAP-Rule:MF_01670};
GN ORFNames=CUC15_16835 {ECO:0000313|EMBL:AXI10496.1};
OS Oceanobacillus zhaokaii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2052660 {ECO:0000313|EMBL:AXI10496.1, ECO:0000313|Proteomes:UP000253908};
RN [1] {ECO:0000313|Proteomes:UP000253908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=160 {ECO:0000313|Proteomes:UP000253908};
RA Zhu W.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01670};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 7/7. {ECO:0000256|HAMAP-
CC Rule:MF_01670}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01670}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01670}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|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; CP024848; AXI10496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345PKG6; -.
DR KEGG; ocn:CUC15_16835; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000253908; 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 {ECO:0000256|HAMAP-Rule:MF_01670};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01670}; Reference proteome {ECO:0000313|Proteomes:UP000253908}.
FT DOMAIN 19..481
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 386
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
SQ SEQUENCE 491 AA; 53588 MW; FA90E1E88F73FE23 CRC64;
MAEVATEVRK LKNYINGEWV ESKATKYEDV YNPATKEVIA RVPISTKEDV DYAAEVAQAA
FEKWSKVSVA KRAKILFSYQ QLLEKNKKEL ARLITIENGK NTTEALGEVG RGIENVEFAA
GIPTLMMGDS LANIATDVEA TNYRYPIGVV GGITPFNFPM MVPAWMFPMA IAAGNSFVLK
PSEKTPLLTE KLAELFSEAG LPNGVLNIVY GAHDVVNGIL DHPDIKAISF VGSQPVGEYV
YKRGSEKLKR VQALTGAKNH SIVLNDADID RAVTDIIGSA FGSAGERCMA CAVVTVQEDV
ADEFISKLTE AADNVKMGNG LDDGVFLGPV IREENQKRTL DYIAKGEAEG ATLVRDGRKD
DLDGGYFVGP TIFEGVTTEM TIWKDEIFAP VLSVIRVKNL KEAIEVANQS EFANGACLFT
TNTSSVRYFR ENIDAGMLGI NLGVPAPMAF FPFSGWKASF YGTLHANGKD SVDFYTRKKV
VTARYETPDF A
//
