Sequence of ADHE_ECOLI
EC Number:1.1.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Other sequences found for EC No. 1.1.1.1
EC Number:1.2.1.10
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
acetaldehyde dehydrogenase (acetylating)
P0A9Q7
Escherichia coli (strain K12)
891
96127
Reaction
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
Other sequences found for EC No. 1.2.1.10
General information:
Sequence
0 MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG
60 IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA
120 IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA
180 LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF
240 DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP
300 AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV
360 AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
420 CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK
480 RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI
540 IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
600 TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME
660 AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG
720 VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
780 HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ
840 CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1026436
Goodlove P.E.,Cunningham P.R.,Parker J.,Clark D.P.
Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli.
Gene
85
209-214
1989
1026437
Kessler D.,Leibrecht I.,Knappe J.
Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.
FEBS Lett.
281
59-63
1991
1026438
Oshima T.,Aiba H.,Baba T.,Fujita K.,Hayashi K.,Honjo A.,Ikemoto K.,Inada T.,Itoh T.,Kajihara M.,Kanai K.,Kashimoto K.,Kimura S.,Kitagawa M.,Makino K.,Masuda S.,Miki T.,Mizobuchi K.,Mori H.,Motomura K.,Nakamura Y.,Nashimoto H.,Nishio Y.,Saito N.,Sampei G.,Seki Y.,Tagami H.,Takemoto K.,Wada C.,Yamamoto Y.,Yano M.,Horiuchi T.
A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.
DNA Res.
3
137-155
1996
1026439
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
1026440
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
1026441
Danchin A.,Krin E.
Filling the gap between hns and adhE in Escherichia coli K12.
Microbiology
141
959-960
1995
1026442
Yamato M.,Takahashi Y.,Tomotake H.,Ota F.,Hirota K.,Yamaguchi K.
Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them.
Microbiol. Immunol.
38
177-182
1994
1026443
Kessler D.,Herth W.,Knappe J.
Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli.
J. Biol. Chem.
267
18073-18079
1992
1026444
Lorowitz W.,Clark D.
Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase.
J. Bacteriol.
152
935-938
1982
1026445
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
1026446
Membrillo-Hernandez J.,Lin E.C.
Regulation of expression of the adhE gene, encoding ethanol oxidoreductase in Escherichia coli: transcription from a downstream promoter and regulation by fnr and RpoS.
J. Bacteriol.
181
7571-7579
1999
1026447
Gupta S.,Mat-Jan F.,Latifi M.,Clark D.P.
Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis.
FEMS Microbiol. Lett.
182
51-55
2000
1026448
Membrillo-Hernandez J.,Echave P.,Cabiscol E.,Tamarit J.,Ros J.,Lin E.C.
Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins.
J. Biol. Chem.
275
33869-33875
2000
1026449
Echave P.,Esparza-Ceron M.A.,Cabiscol E.,Tamarit J.,Ros J.,Membrillo-Hernandez J.,Lin E.C.
DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A.
99
4626-4631
2002
1026450
Echave P.,Tamarit J.,Cabiscol E.,Ros J.
Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli.
J. Biol. Chem.
278
30193-30198
2003
1026451
Nnyepi M.R.,Peng Y.,Broderick J.B.
Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules.
Arch. Biochem. Biophys.
459
1-9
2007
1026452
Zhang J.,Sprung R.,Pei J.,Tan X.,Kim S.,Zhu H.,Liu C.F.,Grishin N.V.,Zhao Y.
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Mol. Cell. Proteomics
8
215-225
2009
1026453
Matuszewska E.,Kwiatkowska J.,Ratajczak E.,Kuczynska-Wisnik D.,Laskowska E.
Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen.
Acta Biochim. Pol.
56
55-61
2009
1026454
Kim G.,Azmi L.,Jang S.,Jung T.,Hebert H.,Roe A.J.,Byron O.,Song J.J.
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Nat. Commun.
10
4527-4527
2019
1026455
Pony P.,Rapisarda C.,Terradot L.,Marza E.,Fronzes R.
Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.
Nat. Commun.
11
1426-1426
2020
1026456
Kim G.,Yang J.,Jang J.,Choi J.S.,Roe A.J.,Byron O.,Seok C.,Song J.J.
Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling.
Commun. Biol.
3
298-298
2020
