ID   ACDH_ECOLI              Reviewed;         316 AA.
AC   P77580; Q2MC73;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 161.
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}; Synonyms=mhpE;
GN   OrderedLocusNames=b0351, JW0342;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Kawamukai M.;
RT   "Complete sequence of the mhp operon.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / CS520;
RX   PubMed=9098055; DOI=10.1128/jb.179.8.2573-2581.1997;
RA   Ferrandez A., Garcia J.L., Diaz E.;
RT   "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT   hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.";
RL   J. Bacteriol. 179:2573-2581(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   INTERACTION WITH MHPF, AND FUNCTION.
RX   PubMed=16782065; DOI=10.1016/j.bbrc.2006.06.009;
RA   Lee S.J., Ko J.H., Kang H.Y., Lee Y.;
RT   "Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia
RT   coli.";
RL   Biochem. Biophys. Res. Commun. 346:1009-1015(2006).
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 3-phenylpropanoate. Functions as a chaperone
CC       protein for folding of MhpE. {ECO:0000269|PubMed:16782065}.
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       ECO:0000269|PubMed:16782065}.
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01657, ECO:0000305}.
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DR   EMBL; D86239; BAA13056.1; -; Genomic_DNA.
DR   EMBL; Y09555; CAA70751.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18075.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73454.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76133.1; -; Genomic_DNA.
DR   PIR; G64762; G64762.
DR   RefSeq; NP_414885.1; NC_000913.3.
DR   RefSeq; WP_000044314.1; NZ_SSZK01000061.1.
DR   AlphaFoldDB; P77580; -.
DR   SMR; P77580; -.
DR   BioGRID; 4261622; 16.
DR   BioGRID; 849402; 10.
DR   DIP; DIP-10210N; -.
DR   IntAct; P77580; 18.
DR   STRING; 511145.b0351; -.
DR   jPOST; P77580; -.
DR   PaxDb; 511145-b0351; -.
DR   EnsemblBacteria; AAC73454; AAC73454; b0351.
DR   GeneID; 66671345; -.
DR   GeneID; 945008; -.
DR   KEGG; ecj:JW0342; -.
DR   KEGG; eco:b0351; -.
DR   PATRIC; fig|1411691.4.peg.1927; -.
DR   EchoBASE; EB3390; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_6; -.
DR   InParanoid; P77580; -.
DR   OMA; QGNVNMV; -.
DR   OrthoDB; 9786743at2; -.
DR   PhylomeDB; P77580; -.
DR   BioCyc; EcoCyc:MHPF-MONOMER; -.
DR   BioCyc; MetaCyc:MHPF-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   PRO; PR:P77580; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..316
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000096471"
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;  33442 MW;  A6918BDA5EF4876B CRC64;
     MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI
     GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI DLTPAAIGPY CVPVVNLEAN
     VDQLNVNMVT CGGQATIPMV AAVSRVARVH YAEIIASIAS KSAGPGTRAN IDEFTETTSR
     AIEVVGGAAK GKAIIVLNPA EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY
     RLKQRVQFEV IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT
     AEKMAQSLAR KAGEAA
//