ADHE_ECOLI
ID ADHE_ECOLI Reviewed; 891 AA.
AC P0A9Q7; P17547;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Bifunctional aldehyde-alcohol dehydrogenase AdhE {ECO:0000305};
DE AltName: Full=Alcohol dehydrogenase E {ECO:0000303|PubMed:12783863};
DE Includes:
DE RecName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000303|PubMed:6752127};
DE Short=ACDH {ECO:0000303|PubMed:9298644};
DE EC=1.2.1.10 {ECO:0000269|PubMed:10612730, ECO:0000269|PubMed:10922373, ECO:0000269|PubMed:17280641, ECO:0000269|PubMed:2015910};
DE Includes:
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:6752127};
DE Short=ADH {ECO:0000303|PubMed:9298644};
DE EC=1.1.1.1 {ECO:0000269|PubMed:10922373, ECO:0000269|PubMed:17280641, ECO:0000269|PubMed:2015910};
GN Name=adhE {ECO:0000303|PubMed:6752127}; Synonyms=ana;
GN OrderedLocusNames=b1241, JW1228;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=2695398; DOI=10.1016/0378-1119(89)90483-6;
RA Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.;
RT "Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-
RT encoding gene of Escherichia coli.";
RL Gene 85:209-214(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=K12;
RX PubMed=2015910; DOI=10.1016/0014-5793(91)80358-a;
RA Kessler D., Leibrecht I., Knappe J.;
RT "Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of
RT Escherichia coli reside on a polymeric protein particle encoded by adhE.";
RL FEBS Lett. 281:59-63(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 849-891.
RC STRAIN=K12;
RX PubMed=7773397; DOI=10.1099/13500872-141-4-959;
RA Danchin A., Krin E.;
RT "Filling the gap between hns and adhE in Escherichia coli K12.";
RL Microbiology 141:959-960(1995).
RN [7]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=7521508; DOI=10.1111/j.1348-0421.1994.tb01762.x;
RA Yamato M., Takahashi Y., Tomotake H., Ota F., Hirota K., Yamaguchi K.;
RT "Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis
RT of the localization of spirosome by use of them.";
RL Microbiol. Immunol. 38:177-182(1994).
RN [8]
RP PROTEIN SEQUENCE OF 2-6 AND 764-768, PROPOSED FUNCTION AS A PFL DEACTIVASE,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=1325457; DOI=10.1016/s0021-9258(19)37154-6;
RA Kessler D., Herth W., Knappe J.;
RT "Ultrastructure and pyruvate formate-lyase radical quenching property of
RT the multienzymic AdhE protein of Escherichia coli.";
RL J. Biol. Chem. 267:18073-18079(1992).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6752127; DOI=10.1128/jb.152.2.935-938.1982;
RA Lorowitz W., Clark D.;
RT "Escherichia coli mutants with a temperature-sensitive alcohol
RT dehydrogenase.";
RL J. Bacteriol. 152:935-938(1982).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10601216; DOI=10.1128/jb.181.24.7571-7579.1999;
RA Membrillo-Hernandez J., Lin E.C.;
RT "Regulation of expression of the adhE gene, encoding ethanol oxidoreductase
RT in Escherichia coli: transcription from a downstream promoter and
RT regulation by fnr and RpoS.";
RL J. Bacteriol. 181:7571-7579(1999).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=10612730; DOI=10.1111/j.1574-6968.2000.tb08872.x;
RA Gupta S., Mat-Jan F., Latifi M., Clark D.P.;
RT "Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia
RT coli is inhibited by intermediates in ubiquinone synthesis.";
RL FEMS Microbiol. Lett. 182:51-55(2000).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ALA-267 AND GLU-568.
RX PubMed=10922373; DOI=10.1074/jbc.m005464200;
RA Membrillo-Hernandez J., Echave P., Cabiscol E., Tamarit J., Ros J.,
RA Lin E.C.;
RT "Evolution of the adhE gene product of Escherichia coli from a functional
RT reductase to a dehydrogenase. Genetic and biochemical studies of the mutant
RT proteins.";
RL J. Biol. Chem. 275:33869-33875(2000).
RN [14]
RP ACTIVITY REGULATION.
RX PubMed=11917132; DOI=10.1073/pnas.072504199;
RA Echave P., Esparza-Ceron M.A., Cabiscol E., Tamarit J., Ros J.,
RA Membrillo-Hernandez J., Lin E.C.;
RT "DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic
RT function and protective role of the chaperone against protein oxidative
RT damage in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4626-4631(2002).
RN [15]
RP FUNCTION AS AN ANTIOXIDANT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12783863; DOI=10.1074/jbc.m304351200;
RA Echave P., Tamarit J., Cabiscol E., Ros J.;
RT "Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli.";
RL J. Biol. Chem. 278:30193-30198(2003).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND LACK OF PFL DEACTIVASE ACTIVITY.
RX PubMed=17280641; DOI=10.1016/j.abb.2006.12.024;
RA Nnyepi M.R., Peng Y., Broderick J.B.;
RT "Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small
RT molecules.";
RL Arch. Biochem. Biophys. 459:1-9(2007).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [18]
RP ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19238259;
RA Matuszewska E., Kwiatkowska J., Ratajczak E., Kuczynska-Wisnik D.,
RA Laskowska E.;
RT "Role of Escherichia coli heat shock proteins IbpA and IbpB in protection
RT of alcohol dehydrogenase AdhE against heat inactivation in the presence of
RT oxygen.";
RL Acta Biochim. Pol. 56:55-61(2009).
RN [19] {ECO:0007744|PDB:6AHC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF COMPACT SPIROSOME,
RP ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF PHE-670.
RC STRAIN=K12;
RX PubMed=31586059; DOI=10.1038/s41467-019-12427-8;
RA Kim G., Azmi L., Jang S., Jung T., Hebert H., Roe A.J., Byron O.,
RA Song J.J.;
RT "Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture
RT critical for its activity.";
RL Nat. Commun. 10:4527-4527(2019).
RN [20] {ECO:0007744|PDB:6TQH, ECO:0007744|PDB:6TQM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF EXTENDED SPIROSOME IN
RP COMPLEXES WITH NAD AND IRON, COFACTOR, ACTIVITY REGULATION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF 446-LYS--GLU-449.
RC STRAIN=K12;
RX PubMed=32188856; DOI=10.1038/s41467-020-15214-y;
RA Pony P., Rapisarda C., Terradot L., Marza E., Fronzes R.;
RT "Filamentation of the bacterial bi-functional alcohol/aldehyde
RT dehydrogenase AdhE is essential for substrate channeling and enzymatic
RT regulation.";
RL Nat. Commun. 11:1426-1426(2020).
RN [21] {ECO:0007744|PDB:7BVP}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF EXTENDED SPIROSOME IN
RP COMPLEX WITH NAD AND ZINC, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=32523125; DOI=10.1038/s42003-020-1030-1;
RA Kim G., Yang J., Jang J., Choi J.S., Roe A.J., Byron O., Seok C.,
RA Song J.J.;
RT "Aldehyde-alcohol dehydrogenase undergoes structural transition to form
RT extended spirosomes for substrate channeling.";
RL Commun. Biol. 3:298-298(2020).
CC -!- FUNCTION: Under fermentative conditions, catalyzes the sequential NADH-
CC dependent reduction of acetyl-CoA to acetaldehyde and then to ethanol
CC (PubMed:6752127, PubMed:2015910, PubMed:10612730, PubMed:10922373,
CC PubMed:17280641). Under aerobic conditions, despite the reversibility
CC of the two NADH-coupled reactions, wild-type E.coli cannot grow on
CC ethanol as the sole carbon and energy source due to the down-regulation
CC of adhE transcription and the inactivation of the enzyme by metal-
CC catalyzed oxidation (MCO) (PubMed:10922373). Nevertheless, in the
CC presence of oxygen, AdhE may act as a hydrogen peroxide scavenger and
CC have a protective role against oxidative stress (PubMed:12783863).
CC {ECO:0000269|PubMed:10612730, ECO:0000269|PubMed:10922373,
CC ECO:0000269|PubMed:12783863, ECO:0000269|PubMed:17280641,
CC ECO:0000269|PubMed:2015910, ECO:0000269|PubMed:6752127}.
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;
CC Evidence={ECO:0000269|PubMed:10612730, ECO:0000269|PubMed:10922373,
CC ECO:0000269|PubMed:17280641, ECO:0000269|PubMed:2015910};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23290;
CC Evidence={ECO:0000305|PubMed:10922373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:10922373, ECO:0000269|PubMed:17280641,
CC ECO:0000269|PubMed:2015910};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292;
CC Evidence={ECO:0000305|PubMed:10922373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:10922373, ECO:0000269|PubMed:17280641,
CC ECO:0000269|PubMed:2015910};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:1325457, ECO:0000269|PubMed:2015910,
CC ECO:0000269|PubMed:32188856};
CC -!- ACTIVITY REGULATION: Formation of filaments, called spirosomes, is
CC critical for activity (PubMed:31586059, PubMed:32188856,
CC PubMed:32523125). Filamentation is essential for substrate channeling
CC between the ALDH and ADH domains and efficient coupling of the ALDH and
CC ADH enzymatic activities, and for the regulation of enzyme activity
CC (PubMed:32188856, PubMed:32523125). In the absence of ligands, the
CC spirosomes are compact (PubMed:31586059, PubMed:32188856,
CC PubMed:32523125). Binding of NAD(+) and Fe(2+) cofactors induces
CC conformational changes and extension of the filaments, leading to the
CC activation of the enzyme (PubMed:31586059, PubMed:32188856,
CC PubMed:32523125). AdhE is inhibited in the presence of oxygen by metal-
CC catalyzed oxidation (MCO) and by heat stress (PubMed:11917132,
CC PubMed:19238259). The chaperone DnaK has a protective effect on AdhE
CC activity under aerobic but not anaerobic conditions (PubMed:11917132).
CC DnaK may protect AdhE and AdhE mutants against irreversible MCO damages
CC and improve their ability to grow aerobically on ethanol
CC (PubMed:11917132). IbpA and IbpB protect AdhE against thermal and
CC oxidative inactivation during oxidative stress, providing that the
CC enzyme remained soluble, and increase the efficiency of reactivation of
CC heat-denatured AdhE by the DnaK system (PubMed:19238259). Acetaldehyde
CC dehydrogenase activity is inhibited by guaiacol, which mimics an
CC intermediate of ubiquinone synthesis (PubMed:10612730).
CC {ECO:0000269|PubMed:10612730, ECO:0000269|PubMed:11917132,
CC ECO:0000269|PubMed:19238259, ECO:0000269|PubMed:31586059,
CC ECO:0000269|PubMed:32188856, ECO:0000269|PubMed:32523125}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 mM for acetaldehyde (for acetaldehyde dehydrogenase activity)
CC {ECO:0000269|PubMed:10922373};
CC KM=240 mM for ethanol (for ethanol dehydrogenase activity)
CC {ECO:0000269|PubMed:10922373};
CC -!- SUBUNIT: Forms long filaments, called spirosomes (PubMed:31586059,
CC PubMed:32188856, PubMed:32523125). Forms rod-like ultrastructures
CC composed of 20-60 identical subunits (PubMed:1325457). Two monomers
CC form a dimer in a head-to-head arm-crossing fashion through the ALDH
CC domains (PubMed:31586059). Subsequently, two dimers form one helical
CC pitch via the interaction of ADH domains in a tail-to-tail manner
CC (PubMed:31586059, PubMed:32523125). These units are further assembled
CC into spirosomes (PubMed:31586059, PubMed:32188856, PubMed:32523125).
CC Formation of these spirosomes is required for activity
CC (PubMed:31586059, PubMed:32188856, PubMed:32523125). Can be isolated in
CC vitro in a wide range of oligomeric states (PubMed:31586059).
CC {ECO:0000269|PubMed:1325457, ECO:0000269|PubMed:31586059,
CC ECO:0000269|PubMed:32188856, ECO:0000269|PubMed:32523125}.
CC -!- INTERACTION:
CC P0A9Q7; P0A9Q7: adhE; NbExp=2; IntAct=EBI-543417, EBI-543417;
CC P0A9Q7; P0A7V0: rpsB; NbExp=2; IntAct=EBI-543417, EBI-543439;
CC -!- INDUCTION: Expression is about 10-fold higher during anaerobic than
CC during aerobic growth (PubMed:10601216). Contains two transcriptional
CC start sites, which are both functional. Both start sites are NarL
CC repressible in the presence of nitrate and activited by RpoS. Fis is
CC required only for transcriptional initiation from the upstream start
CC site. Fnr can regulate expression from the downstream transcriptional
CC start site only in the physical absence of the upstream region
CC (PubMed:10601216). However, under all experimental conditions tested,
CC only the upstream start site is active and acts as a silencer of
CC downstream transcription (PubMed:10601216). Translation of the mRNA
CC starting at the upstream site, but not the one starting atthe
CC downstream site, requires RNase III (PubMed:10601216).
CC {ECO:0000269|PubMed:10601216}.
CC -!- DOMAIN: Contains an N-terminal aldehyde dehydrogenase (ALDH) domain and
CC a C-terminal iron-dependent alcohol dehydrogenase (ADH) domain,
CC interconnected by a short linker (PubMed:31586059, PubMed:32188856).
CC ALDH and ADH activities are topologically separated in the compact
CC spirosome architecture (PubMed:31586059). {ECO:0000269|PubMed:31586059,
CC ECO:0000269|PubMed:32188856}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cannot grow aerobically in
CC minimal media, is extremely sensitive to oxidative stress and shows
CC morphologic defects that are associated with deficient septum formation
CC (PubMed:12783863). In addition, mutant displays increased levels of
CC internal peroxides and increased protein carbonyl content
CC (PubMed:12783863). Both acetaldehyde dehydrogenase and alcohol
CC dehydrogenase activities are thermolabile in temperature-sensitive
CC mutants (PubMed:6752127). {ECO:0000269|PubMed:12783863,
CC ECO:0000269|PubMed:6752127}.
CC -!- MISCELLANEOUS: Has previously been proposed to have pyruvate formate-
CC lyase (PFL) deactivase activity and to catalyze the quenching of the
CC PFL radical in an Fe(2+), NAD and CoA dependent reaction
CC (PubMed:2015910, PubMed:1325457). However, it was shown later that AdhE
CC does not catalyze the deactivation of active PFL (PubMed:17280641).
CC Inactivation of PFL is attributed to the CoA and Fe(II) present, which
CC appear to increase the rate of deactivation (PubMed:17280641).
CC {ECO:0000269|PubMed:1325457, ECO:0000269|PubMed:17280641,
CC ECO:0000269|PubMed:2015910}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000305}.
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DR EMBL; X59263; CAA41955.1; -; Genomic_DNA.
DR EMBL; M33504; AAA23420.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36121.1; -; Genomic_DNA.
DR EMBL; X67326; CAA47743.1; -; Genomic_DNA.
DR PIR; JS0406; DEEC.
DR RefSeq; NP_415757.1; NC_000913.3.
DR RefSeq; WP_000301651.1; NZ_STEB01000005.1.
DR PDB; 6AHC; EM; 3.45 A; A/B/C/D/E/F/G/H=1-891.
DR PDB; 6TQH; EM; 3.40 A; A/B/C/F=1-891.
DR PDB; 6TQM; EM; 3.80 A; A/B/C/F=1-891.
DR PDB; 7BVP; EM; 3.45 A; A/B/C/D/E/F=1-891.
DR PDBsum; 6AHC; -.
DR PDBsum; 6TQH; -.
DR PDBsum; 6TQM; -.
DR PDBsum; 7BVP; -.
DR AlphaFoldDB; P0A9Q7; -.
DR SASBDB; P0A9Q7; -.
DR SMR; P0A9Q7; -.
DR BioGRID; 4259605; 5.
DR BioGRID; 850204; 1.
DR DIP; DIP-35790N; -.
DR IntAct; P0A9Q7; 21.
DR MINT; P0A9Q7; -.
DR STRING; 511145.b1241; -.
DR MoonProt; P0A9Q7; -.
DR iPTMnet; P0A9Q7; -.
DR jPOST; P0A9Q7; -.
DR PaxDb; P0A9Q7; -.
DR PRIDE; P0A9Q7; -.
DR EnsemblBacteria; AAC74323; AAC74323; b1241.
DR EnsemblBacteria; BAA36121; BAA36121; BAA36121.
DR GeneID; 66674939; -.
DR GeneID; 945837; -.
DR KEGG; ecj:JW1228; -.
DR KEGG; eco:b1241; -.
DR PATRIC; fig|1411691.4.peg.1043; -.
DR EchoBASE; EB0030; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_2_2_6; -.
DR InParanoid; P0A9Q7; -.
DR OMA; QWFKVPP; -.
DR PhylomeDB; P0A9Q7; -.
DR BioCyc; EcoCyc:ADHE-MON; -.
DR BioCyc; MetaCyc:ADHE-MON; -.
DR PRO; PR:P0A9Q7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:EcoCyc.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IMP:EcoliWiki.
DR GO; GO:0004025; F:alcohol dehydrogenase activity, iron-dependent; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0006115; P:ethanol biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0019664; P:mixed acid fermentation; IMP:EcoCyc.
DR GO; GO:0051260; P:protein homooligomerization; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR CDD; cd08178; AAD_C; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Iron; Metal-binding;
KW Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2015910,
FT ECO:0000269|PubMed:2695398, ECO:0000269|PubMed:7521508"
FT CHAIN 2..891
FT /note="Bifunctional aldehyde-alcohol dehydrogenase AdhE"
FT /id="PRO_0000087837"
FT REGION 2..440
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000305"
FT REGION 441..448
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:31586059"
FT REGION 449..891
FT /note="Alcohol dehydrogenase"
FT /evidence="ECO:0000305"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HTJ1"
FT BINDING 110..115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 419
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 487
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 519
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 546..550
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 610
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 619
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32523125,
FT ECO:0007744|PDB:7BVP"
FT BINDING 653
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32188856,
FT ECO:0000305|PubMed:32523125, ECO:0007744|PDB:6TQH,
FT ECO:0007744|PDB:6TQM"
FT BINDING 657
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32188856,
FT ECO:0000305|PubMed:32523125, ECO:0007744|PDB:6TQH,
FT ECO:0007744|PDB:6TQM"
FT BINDING 723
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32188856,
FT ECO:0000305|PubMed:32523125, ECO:0007744|PDB:6TQH,
FT ECO:0007744|PDB:6TQM"
FT BINDING 737
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32188856,
FT ECO:0000305|PubMed:32523125, ECO:0007744|PDB:6TQH,
FT ECO:0007744|PDB:6TQM"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 267
FT /note="A->T: Shows aerobic growth ability on ethanol. Shows
FT 5-6 fold increase in acetaldehyde dehydrogenase activity,
FT but does not affect ethanol dehydrogenase activity. Shows
FT decreased thermal enzyme stability and increased
FT sensitivity to MCO damage. Shows increased protein
FT stability and resistance to MCO; when associated with K-
FT 568."
FT /evidence="ECO:0000269|PubMed:10922373"
FT MUTAGEN 446..449
FT /note="Missing: Can form dimers, but does not assemble into
FT long filaments. Strongly affects ALDH activity, but not ADH
FT activity."
FT /evidence="ECO:0000269|PubMed:32188856"
FT MUTAGEN 568
FT /note="E->K: Partially restores protein stability and
FT resistance to MCO damage; when associated with T-267."
FT /evidence="ECO:0000269|PubMed:10922373"
FT MUTAGEN 670
FT /note="F->A,E,V: Disrupts spirosome formation. Affects the
FT forward activity of ALDH."
FT /evidence="ECO:0000269|PubMed:31586059"
FT HELIX 6..23
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 62..80
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:6AHC"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6AHC"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7BVP"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 294..298
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:7BVP"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6AHC"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 467..474
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 522..535
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:7BVP"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 547..560
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:6AHC"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:7BVP"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:6AHC"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:6AHC"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 644..662
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 672..679
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 680..684
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 686..691
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 697..714
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 722..729
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 737..752
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:7BVP"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:6AHC"
FT HELIX 771..774
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 776..782
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 793..807
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:6TQH"
FT TURN 826..828
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 830..837
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:6TQH"
FT STRAND 845..847
FT /evidence="ECO:0007829|PDB:7BVP"
FT HELIX 851..854
FT /evidence="ECO:0007829|PDB:6TQH"
FT HELIX 856..862
FT /evidence="ECO:0007829|PDB:6TQH"
SQ SEQUENCE 891 AA; 96127 MW; 75469F57419C8C79 CRC64;
MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG
IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA
IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF
DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV
AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK
RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME
AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG
VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ
CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A
