ID   ACDH_SPHYA              Reviewed;         312 AA.
AC   A2TC44;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
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=xylQ;
OS   Sphingobium yanoikuyae (Sphingomonas yanoikuyae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=13690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6900 / JCM 10274 / B1;
RX   PubMed=17647036; DOI=10.1007/s10295-007-0235-3;
RA   Chadhain S.M., Moritz E.M., Kim E., Zylstra G.J.;
RT   "Identification, cloning, and characterization of a multicomponent biphenyl
RT   dioxygenase from Sphingobium yanoikuyae B1.";
RL   J. Ind. Microbiol. Biotechnol. 34:605-613(2007).
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; EF151283; ABM79796.1; -; Genomic_DNA.
DR   RefSeq; WP_037508677.1; NZ_KL662202.1.
DR   AlphaFoldDB; A2TC44; -.
DR   SMR; A2TC44; -.
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..312
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387745"
FT   ACT_SITE        129
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         11..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         160..168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   312 AA;  33009 MW;  C4E7509F7F064B2D CRC64;
     MTKMKCAIIG SGNIGTDLMI KLLKGSDTLE LAAVVGIDPA SEGLAMARER GVATTHEGIE
     GLRKLPAYPE IGIAFDATSA YAHKEHDAAL QADGKLVVDL TPAAIGPFFV PPVGGVLDSE
     IRNVNMVTCG GQATIPIVAA VSRVTPVHYA EIVASVSSRS AGPGTRANID EFTRTTAQAI
     EIVGGAGRGR AIIILNPAEP PMIMRDTIFT LTDQVDEDAI RASVKEMVET VQAYVPGYRL
     KQEVQFERFG SNRPLKIPGY GEFVGLKTSV FLEVEGAGDY LPKYSGNLDI MTAAAKAAGE
     RLAQQRLEKV AA