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P0A9Q7

- ADHE_ECOLI

UniProt

P0A9Q7 - ADHE_ECOLI

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Protein

Aldehyde-alcohol dehydrogenase

Gene
adhE, ana, b1241, JW1228
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.
Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.

Cofactori

Iron.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei246 – 2461 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi422 – 4276NAD Reviewed prediction

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: EcoliWiki
  2. alcohol dehydrogenase (NAD) activity Source: EcoliWiki
  3. identical protein binding Source: IntAct
  4. metal ion binding Source: InterPro

GO - Biological processi

  1. carbon utilization Source: InterPro
  2. ethanol biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, NAD

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde-alcohol dehydrogenase
Including the following 3 domains:
Alcohol dehydrogenase (EC:1.1.1.1)
Short name:
ADH
Acetaldehyde dehydrogenase [acetylating] (EC:1.2.1.10)
Short name:
ACDH
Pyruvate-formate-lyase deactivase
Short name:
PFL deactivase
Gene namesi
Name:adhE
Synonyms:ana
Ordered Locus Names:b1241, JW1228
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10031. adhE.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 891890Aldehyde-alcohol dehydrogenasePRO_0000087837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei358 – 3581N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A9Q7.
PRIDEiP0A9Q7.

Expressioni

Inductioni

Under anaerobic conditions in the absence of nitrate.

Gene expression databases

GenevestigatoriP0A9Q7.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-543417,EBI-543417

Protein-protein interaction databases

BioGridi850204. 1 interaction.
DIPiDIP-35790N.
IntActiP0A9Q7. 18 interactions.
MINTiMINT-1288364.
STRINGi511145.b1241.

Structurei

3D structure databases

ProteinModelPortaliP0A9Q7.
SMRiP0A9Q7. Positions 3-448, 450-864.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000025256.
KOiK04072.
OMAiSPLLAMY.
OrthoDBiEOG6TFCQS.
PhylomeDBiP0A9Q7.

Family and domain databases

Gene3Di3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProiIPR001670. 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]
PfamiPF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view]
PIRSFiPIRSF000111. ALDH_ADH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9Q7-1 [UniParc]FASTAAdd to Basket

« Hide

MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA    50
KMAVAESGMG IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI 100
AEPIGIICGI VPTTNPTSTA IFKSLISLKT RNAIIFSPHP RAKDATNKAA 150
DIVLQAAIAA GAPKDLIGWI DQPSVELSNA LMHHPDINLI LATGGPGMVK 200
AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF DNGVICASEQ 250
SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP 300
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE 350
DAVEKAEKLV AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA 400
SQGGIGDLYN FKLAPSLTLG CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN 450
MLWHKLPKSI YFRRGSLPIA LDEVITDGHK RALIVTDRFL FNNGYADQIT 500
SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI IALGGGSPMD 550
AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG 600
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG 650
GLDAVTHAME AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR 700
ERVHSAATIA GIAFANAFLG VCHSMAHKLG SQFHIPHGLA NALLICNVIR 750
YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD HLGLSAPGDR TAAKIEKLLA 800
WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ CTGANPRYPL 850
ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A 891
Length:891
Mass (Da):96,127
Last modified:January 23, 2007 - v2
Checksum:i75469F57419C8C79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiJS0406. DEEC.
RefSeqiNP_415757.1. NC_000913.3.
YP_489507.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74323; AAC74323; b1241.
BAA36121; BAA36121; BAA36121.
GeneIDi12930611.
945837.
KEGGiecj:Y75_p1213.
eco:b1241.
PATRICi32117740. VBIEscCol129921_1290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi JS0406. DEEC.
RefSeqi NP_415757.1. NC_000913.3.
YP_489507.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A9Q7.
SMRi P0A9Q7. Positions 3-448, 450-864.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 850204. 1 interaction.
DIPi DIP-35790N.
IntActi P0A9Q7. 18 interactions.
MINTi MINT-1288364.
STRINGi 511145.b1241.

Proteomic databases

PaxDbi P0A9Q7.
PRIDEi P0A9Q7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74323 ; AAC74323 ; b1241 .
BAA36121 ; BAA36121 ; BAA36121 .
GeneIDi 12930611.
945837.
KEGGi ecj:Y75_p1213.
eco:b1241.
PATRICi 32117740. VBIEscCol129921_1290.

Organism-specific databases

EchoBASEi EB0030.
EcoGenei EG10031. adhE.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000025256.
KOi K04072.
OMAi SPLLAMY.
OrthoDBi EOG6TFCQS.
PhylomeDBi P0A9Q7.

Enzyme and pathway databases

BioCyci EcoCyc:ADHE-MONOMER.
ECOL316407:JW1228-MONOMER.
MetaCyc:ADHE-MONOMER.

Miscellaneous databases

PROi P0A9Q7.

Gene expression databases

Genevestigatori P0A9Q7.

Family and domain databases

Gene3Di 3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProi IPR001670. 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 ]
Pfami PF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000111. ALDH_ADH. 1 hit.
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiADHE_ECOLI
AccessioniPrimary (citable) accession number: P0A9Q7
Secondary accession number(s): P17547
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi