ID   ACDH3_PARXL             Reviewed;         313 AA.
AC   Q13QH7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Acetaldehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] 3 {ECO:0000255|HAMAP-Rule:MF_01657};
GN   OrderedLocusNames=Bxeno_B0694; ORFNames=Bxe_B2326;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33662.1; -; Genomic_DNA.
DR   RefSeq; WP_011491022.1; NZ_CP008762.1.
DR   AlphaFoldDB; Q13QH7; -.
DR   SMR; Q13QH7; -.
DR   STRING; 266265.Bxe_B2326; -.
DR   EnsemblBacteria; ABE33662; ABE33662; Bxe_B2326.
DR   KEGG; bxb:DR64_4658; -.
DR   KEGG; bxe:Bxe_B2326; -.
DR   PATRIC; fig|266265.5.peg.5386; -.
DR   eggNOG; COG4569; Bacteria.
DR   OMA; MIKVIRH; -.
DR   OrthoDB; 1432332at2; -.
DR   Proteomes; UP000001817; Chromosome 2.
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..313
FT                   /note="Acetaldehyde dehydrogenase 3"
FT                   /id="PRO_0000337977"
FT   ACT_SITE        133
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         13..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         164..172
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   313 AA;  32763 MW;  F0A85325E5E6BAD5 CRC64;
     MASEKLKAAI IGSGNIGTDL MIKIMRHSEH LEMAAMVGID AASDGLARAA RLGVATTHEG
     VEGLTRLPVF DDIDFVFDAT SAGAHVKNDA FLRALKPGIR LIDLTPAAIG PYCVPVVNLD
     AHLDSRNVNM VTCGGQATIP MVAAVSRVAK VHYAEIVASI SSKSAGPGTR ANIDEFTETT
     SKAIEAVGGA AKGKAIIVLN PAEPPVMMRD TVYVLSDLAD RAQVEASIEA MAAAVHAYVP
     GYRLKQKVQF DEIAADVPLN IPGLGRFSGL KTSVFIEVEG AAHYLPAYAG NLDIMTSAAL
     ATAERMAQSL VQA