ID W4Q3R4_9BACI Unreviewed; 295 AA.
AC W4Q3R4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000256|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000256|HAMAP-Rule:MF_01657};
GN ORFNames=JCM9140_2672 {ECO:0000313|EMBL:GAE26590.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE26590.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE26590.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE26590.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}.
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:GAE26590.1}.
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DR EMBL; BAUT01000027; GAE26590.1; -; Genomic_DNA.
DR RefSeq; WP_034746487.1; NZ_BAZN01000027.1.
DR AlphaFoldDB; W4Q3R4; -.
DR STRING; 1236970.JCM9140_2672; -.
DR OrthoDB; 9786743at2; -.
DR Proteomes; UP000018890; Unassembled WGS sequence.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR InterPro; IPR015426; Acetylaldehyde_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR03215; ac_ald_DH_ac; 1.
DR Pfam; PF09290; AcetDehyd-dimer; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01657};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657};
KW Reference proteome {ECO:0000313|Proteomes:UP000018890}.
FT DOMAIN 5..119
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 127
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 11..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 158..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 295 AA; 31674 MW; 44C8F81A7F384F9B CRC64;
MDKIKVAIIG TGNIGTDLML KIERSSSLKL TSLIGIDPYS DGVKRAKERG YQTFTNGLEE
FLETSSELAD IFFDATSAKA HVRHAKLLKE AGKQVLDLTP AARGPFVVPP VNLDSNLDVP
NINLITCGGQ ATIPMVHAVN RVAPVEYAEI VATISSESAG PGTRANIDEF TQTTKRGIEE
IGGAKQGKAI IILNPAEPPI LMRDTVYAVV EPGKMDEAAI TKSIKEMADS VQSYVPGYRL
RTKPIFDGNR VTIFLEVEGA GDYLPSYSGN LDIMTAAAVK VAEELAKNKL NSAII
//
