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P0A9Q7

- ADHE_ECOLI

UniProt

P0A9Q7 - ADHE_ECOLI

Protein

Aldehyde-alcohol dehydrogenase

Gene

adhE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 – 2461By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi422 – 4276NADSequence Analysis

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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

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    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

    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: October 1, 2014
    This is version 86 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