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P0A9Q7 (ADHE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde-alcohol dehydrogenase

Including the following 3 domains:

  1. Alcohol dehydrogenase
    Short name=ADH
    EC=1.1.1.1
  2. Acetaldehyde dehydrogenase [acetylating]
    Short name=ACDH
    EC=1.2.1.10
  3. Pyruvate-formate-lyase deactivase
    Short name=PFL deactivase
Gene names
Name:adhE
Synonyms:ana
Ordered Locus Names:b1241, JW1228
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length891 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.

Cofactor

Iron.

Subunit structure

Seems to form a rod shaped polymer composed of about 40 identical subunits.

Induction

Under anaerobic conditions in the absence of nitrate.

Sequence similarities

In the N-terminal section; belongs to the aldehyde dehydrogenase family.

In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-543417,EBI-543417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2 Ref.7
Chain2 – 891890Aldehyde-alcohol dehydrogenase
PRO_0000087837

Regions

Nucleotide binding422 – 4276NAD Potential

Sites

Active site2461 By similarity

Amino acid modifications

Modified residue3581N6-acetyllysine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P0A9Q7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 75469F57419C8C79

FASTA89196,127
        10         20         30         40         50         60 
MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG 

        70         80         90        100        110        120 
IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA 

       130        140        150        160        170        180 
IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA 

       190        200        210        220        230        240 
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF 

       250        260        270        280        290        300 
DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP 

       310        320        330        340        350        360 
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV 

       370        380        390        400        410        420 
AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG 

       430        440        450        460        470        480 
CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK 

       490        500        510        520        530        540 
RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI 

       550        560        570        580        590        600 
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG 

       610        620        630        640        650        660 
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME 

       670        680        690        700        710        720 
AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG 

       730        740        750        760        770        780 
VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD 

       790        800        810        820        830        840 
HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ 

       850        860        870        880        890 
CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli."
Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.
Gene 85:209-214(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
[2]"Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE."
Kessler D., Leibrecht I., Knappe J.
FEBS Lett. 281:59-63(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION.
Strain: K12.
[3]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Filling the gap between hns and adhE in Escherichia coli K12."
Danchin A., Krin E.
Microbiology 141:959-960(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 849-891.
Strain: K12.
[7]"Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them."
Yamato M., Takahashi Y., Tomotake H., Ota F., Hirota K., Yamaguchi K.
Microbiol. Immunol. 38:177-182(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli."
Echave P., Tamarit J., Cabiscol E., Ros J.
J. Biol. Chem. 278:30193-30198(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ANTIOXIDANT ROLE OF ADHE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59263 Genomic DNA. Translation: CAA41955.1.
M33504 Genomic DNA. Translation: AAA23420.1.
U00096 Genomic DNA. Translation: AAC74323.1.
AP009048 Genomic DNA. Translation: BAA36121.1.
X67326 Genomic DNA. Translation: CAA47743.1.
PIRDEEC. JS0406.
RefSeqNP_415757.1. NC_000913.3.
YP_489507.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9Q7.
SMRP0A9Q7. Positions 3-448, 450-864.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid850204. 1 interaction.
DIPDIP-35790N.
IntActP0A9Q7. 18 interactions.
MINTMINT-1288364.
STRING511145.b1241.

Proteomic databases

PaxDbP0A9Q7.
PRIDEP0A9Q7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74323; AAC74323; b1241.
BAA36121; BAA36121; BAA36121.
GeneID12930611.
945837.
KEGGecj:Y75_p1213.
eco:b1241.
PATRIC32117740. VBIEscCol129921_1290.

Organism-specific databases

EchoBASEEB0030.
EcoGeneEG10031. adhE.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000025256.
KOK04072.
OMASPLLAMY.
OrthoDBEOG6TFCQS.
PhylomeDBP0A9Q7.

Enzyme and pathway databases

BioCycEcoCyc:ADHE-MONOMER.
ECOL316407:JW1228-MONOMER.
MetaCyc:ADHE-MONOMER.

Gene expression databases

GenevestigatorP0A9Q7.

Family and domain databases

Gene3D3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012079. Bifunc_Ald/ADH.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view]
PIRSFPIRSF000111. ALDH_ADH. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0A9Q7.

Entry information

Entry nameADHE_ECOLI
AccessionPrimary (citable) accession number: P0A9Q7
Secondary accession number(s): P17547
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene