ID   ACDH_VEREI              Reviewed;         303 AA.
AC   A1WLL3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657};
GN   OrderedLocusNames=Veis_2782;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC         Rule:MF_01657};
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR   EMBL; CP000542; ABM58520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1WLL3; -.
DR   SMR; A1WLL3; -.
DR   STRING; 391735.Veis_2782; -.
DR   EnsemblBacteria; ABM58520; ABM58520; Veis_2782.
DR   KEGG; vei:Veis_2782; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_4; -.
DR   OMA; TSAYVHK; -.
DR   Proteomes; UP000000374; Chromosome.
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   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   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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387750"
FT   ACT_SITE        130
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         161..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         272
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   303 AA;  32263 MW;  BC5FACC2F10AC3A4 CRC64;
     MKKIKCALIG PGNIGTDLLA KLQRSPVLEP VWMVGIDPAS DGLKRASEMG IKTTAEGVDG
     LIPHMKADGV QIVFDATSAY VHAENSAKVN AQGAMMIDLT PAAIGPYCVP PVNLKQHVGR
     REMNVNMVTC GGQATIPMVY AVSRVQPVAY GEIVATVSSR SVGPGTRKNI DEFTRTTAGA
     VEKVGGARQG KAIIIINPAE PPLIMRDTVH CLVEGKPDEA AITQSIHDMI REVQKYVPGY
     KLVNGPVFDG QRVSVFMEVE GLGDYLPKYA GNLDIMTAAA ARTAEMFAEE ILKGELVLEP
     VAA