ID   ACDH_POLSJ              Reviewed;         314 AA.
AC   Q120P0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Bpro_5135;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OG   Plasmid pPol360.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000317; ABE47002.1; -; Genomic_DNA.
DR   RefSeq; WP_011485985.1; NC_007949.1.
DR   AlphaFoldDB; Q120P0; -.
DR   SMR; Q120P0; -.
DR   EnsemblBacteria; ABE47002; ABE47002; Bpro_5135.
DR   KEGG; pol:Bpro_5135; -.
DR   HOGENOM; CLU_062208_0_0_4; -.
DR   OMA; TSAYVHK; -.
DR   OrthoDB; 1432332at2; -.
DR   Proteomes; UP000001983; Plasmid pPol360.
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; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387704"
FT   ACT_SITE        132
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         14..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         163..171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   314 AA;  32808 MW;  7394F6A96D63FA43 CRC64;
     MTKSQRLQVA IIGSGNIGTD LMIKVMRNSK HLSMGAMVGI DAASDGLARA GRLGVPVTHE
     GITGLVGLPN FGDIRIAFDA TSAGAHAGHN EVLQRHGVKV IDLTPAAIGP YVIPVVNLEE
     QLSSPNINMV TCGGQATIPI VRAVSQIARV RYAEIVASIA SKSAGPGTRA NIDEFTETTS
     AAIVSVGRAE HGKAIIVLNP AEPSLMMRDT VFCLVDADAD QEAIRLSVRD MVRSVAAYVP
     GYRLKQDVQF DVIPDKAPVN VPGIGRVSGL KVSVFLEVEG AAHYLPAYAG NLDIMTSAAL
     AAADKIAASL ITAR