ID   ACDH_PSEST              Reviewed;         307 AA.
AC   Q9ZI57;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AN10;
RX   PubMed=10713446; DOI=10.1016/s0378-1119(00)00038-x;
RA   Bosch R., Garcia-Valdes E., Moore E.R.B.;
RT   "Complete nucleotide sequence and evolutionary significance of a
RT   chromosomally encoded naphthalene-degradation lower pathway from
RT   Pseudomonas stutzeri AN10.";
RL   Gene 245:65-74(2000).
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; AF039534; AAD02152.1; -; Genomic_DNA.
DR   RefSeq; WP_003292099.1; NZ_POUI01000002.1.
DR   AlphaFoldDB; Q9ZI57; -.
DR   SMR; Q9ZI57; -.
DR   OrthoDB; 1432332at2; -.
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..307
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387711"
FT   ACT_SITE        131
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         162..170
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   307 AA;  32956 MW;  6F122F1E872A798C CRC64;
     MSKKLKAAII GPGNIGTDLV MKMLRSEWIE PVWMVGIDPE SDGLKRAREF GLKTTAEGVD
     GLLPHVLEDD IRIAFDATSA YVHAENSRKL NELGVLMVDL TPAAIGPYCV PPVNLKQHVG
     TLEMNVNMVT CGGQATIPMV AAVSRVQPVA YGEIVATVSS RSIGPGTRKN IDEFTRTTAG
     AIEQVGGAKE GKAIIVVNPA EPPLMMRDTI HCLTETEPDQ DAITASVHAM IAEVQKYVPG
     YRLKNGPVFD GNRVSIFMEV EGLGDYLPKY AGNLDIMTAA ALRTGEMFAE EIASGTIQLP
     RREAALA