ID   ACDH_BACPJ              Reviewed;         302 AA.
AC   Q764S1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Name=nahO;
OS   Bacillus sp. (strain JF8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1921421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15073308; DOI=10.1099/mic.0.26858-0;
RA   Miyazawa D., Mukerjee-Dhar G., Shimura M., Hatta T., Kimbara K.;
RT   "Genes for Mn(II)-dependent NahC and Fe(II)-dependent NahH located in close
RT   proximity in the thermophilic naphthalene and PCB degrader, Bacillus sp.
RT   JF8: cloning and characterization.";
RL   Microbiology 150:993-1004(2004).
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; AB116258; BAD08310.1; -; Genomic_DNA.
DR   RefSeq; WP_020960483.1; NC_022080.4.
DR   AlphaFoldDB; Q764S1; -.
DR   SMR; Q764S1; -.
DR   STRING; 1921421.M493_12200; -.
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.
FT   CHAIN           1..302
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387625"
FT   ACT_SITE        127
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         12..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         158..166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         276
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   302 AA;  32513 MW;  DB9686FCD895A115 CRC64;
     MNRTVKVAIL GSGNIGTDLM YKILKKRWVL ELSMIAGIDP QSEGLARARA EGVYATAGGI
     DAILEDPEIK IVFDATSAKA HLKHAKRLKE AGKVAIDLTP AAVGPYVVPP VNLMEHVDKD
     NVNLITCGGQ ATIPLVYAVS RVANVKYAEM VSTVSSSSAG PGTRQNIDEF TFTTSRGLEV
     IGGAEKGKAI IILNPAKPPI LMRNTVYIAY EDGDDHQIRH SIGQMIHDVQ QYVPGYRLKG
     EPIFDRRETP KGRLDVVILL LEVEGAGDFL PVSAGNLDIM TASAKQVGEV IAKRLIEMTS
     TA