ID A0A0Q9SS91_9BACL Unreviewed; 481 AA.
AC A0A0Q9SS91;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=iolA {ECO:0000256|HAMAP-Rule:MF_01670};
GN ORFNames=ASG93_27585 {ECO:0000313|EMBL:KRF30495.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF30495.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF30495.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF30495.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF30495.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF30495.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRF30495.1}.
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DR EMBL; LMSP01000013; KRF30495.1; -; Genomic_DNA.
DR RefSeq; WP_056833596.1; NZ_LMSP01000013.1.
DR AlphaFoldDB; A0A0Q9SS91; -.
DR STRING; 1736411.ASG93_27585; -.
DR OrthoDB; 20170at2; -.
DR UniPathway; UPA00076; UER00148.
DR Proteomes; UP000051948; Unassembled WGS sequence.
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}.
FT DOMAIN 13..477
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01670"
SQ SEQUENCE 481 AA; 52554 MW; C74AF390DB6144E3 CRC64;
MTTTLKNWIG GEWIASTSTQ TEPVYNPATE EILAHIPIST KDDVDHAVRT AQEAFQTWSR
TPVPRRARVL FKYQQLLVEH WDELARIVTQ ENGKSYNEAY GEVLRGIECV EFAAGAPSLM
MGKQLPDIAS NIESGMYRYP IGVIGGITPF NFPMMVPCWM FPLAIACGNT FVLKPSERTP
HLANRLAELF HEAGLPAGVL NIVHGAHDVV NGLLEHKEVK AISFVGSQPV AEYIYKTASA
NGKRVQALAG AKNHSIVMPD ADLNIAVKEI VNAAFGSAGE RCMACSVVVA VGEVGDTLVG
KLLEAADKIT IGNGLEEGIF LGPVIRGQHK ERTLKYIEIG ETEGALLVRD GRKDAASEGQ
GYFVGPTIFD QVECGMKIWE DEIFAPVLSI VRVATLEEAI ELSNRSDFAN GACLFTKDGS
NVRQFRENID AGMLGINLGV PAPMAFFPFS GWKKSFYGDL HANGTDGVEF YTRKKMVTAR
W
//
