ID ACDH_ECOLU Reviewed; 316 AA.
AC B7N8Q8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=mhpF {ECO:0000255|HAMAP-Rule:MF_01657}; OrderedLocusNames=ECUMN_0394;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using
CC NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway
CC for the degradation of aromatic compounds. {ECO:0000255|HAMAP-
CC Rule:MF_01657}.
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 -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01657}.
CC -!- SUBUNIT: Interacts with MhpE. {ECO:0000255|HAMAP-Rule:MF_01657}.
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU928163; CAR11609.1; -; Genomic_DNA.
DR RefSeq; WP_000044321.1; NC_011751.1.
DR RefSeq; YP_002411157.1; NC_011751.1.
DR AlphaFoldDB; B7N8Q8; -.
DR SMR; B7N8Q8; -.
DR STRING; 585056.ECUMN_0394; -.
DR KEGG; eum:ECUMN_0394; -.
DR PATRIC; fig|585056.7.peg.592; -.
DR HOGENOM; CLU_062208_0_0_6; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000007097; Chromosome.
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:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR03215; ac_ald_DH_ac; 1.
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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT CHAIN 1..316
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_1000187034"
FT ACT_SITE 131
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 162..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 316 AA; 33501 MW; 083E370E5BE355A8 CRC64;
MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI
GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI DLTPAAIGPY CVPVVNLEEN
VDQLNVNMVT CGGQATIPMV AAVSRVARVH YAEIIASIAS KSAGPGTRAN IDEFTETTSR
AIEVVGGAAK GKAIIVLNPA EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY
RLKQRVQFEV IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT
AEKMAQSLAR KAGEAA
//
