ACDH_ECOLI
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 03-AUG-2022, entry version 154.
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; Proteobacteria; 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; P77580; -.
DR PRIDE; P77580; -.
DR EnsemblBacteria; AAC73454; AAC73454; b0351.
DR EnsemblBacteria; BAE76133; BAE76133; BAE76133.
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; TSAYVHK; -.
DR PhylomeDB; P77580; -.
DR BioCyc; EcoCyc:MHPF-MON; -.
DR BioCyc; MetaCyc:MHPF-MON; -.
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 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 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
