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P0A9Q8

- ADHE_ECO57

UniProt

P0A9Q8 - ADHE_ECO57

Protein

Aldehyde-alcohol dehydrogenase

Gene

adhE

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Iron.By similarity

    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: UniProtKB-EC
    2. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
    3. metal ion binding Source: InterPro

    GO - Biological processi

    1. alcohol metabolic process Source: InterPro
    2. carbon utilization Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, NAD

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-1725-MONOMER.
    ECOO157: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
    Ordered Locus Names:Z2016, ECs1741
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 891890Aldehyde-alcohol dehydrogenasePRO_0000087838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei358 – 3581N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP0A9Q8.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    MINTiMINT-1288351.
    STRINGi155864.Z2016.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A9Q8.
    SMRiP0A9Q8. 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.

    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.

    P0A9Q8-1 [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
    AE005174 Genomic DNA. Translation: AAG56096.1.
    BA000007 Genomic DNA. Translation: BAB35164.1.
    PIRiE90846.
    RefSeqiNP_287484.1. NC_002655.2.
    NP_309768.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG56096; AAG56096; Z2016.
    BAB35164; BAB35164; BAB35164.
    GeneIDi913110.
    960491.
    KEGGiece:Z2016.
    ecs:ECs1741.
    PATRICi18352746. VBIEscCol44059_1596.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56096.1 .
    BA000007 Genomic DNA. Translation: BAB35164.1 .
    PIRi E90846.
    RefSeqi NP_287484.1. NC_002655.2.
    NP_309768.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0A9Q8.
    SMRi P0A9Q8. Positions 3-448, 450-864.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1288351.
    STRINGi 155864.Z2016.

    Proteomic databases

    PRIDEi P0A9Q8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG56096 ; AAG56096 ; Z2016 .
    BAB35164 ; BAB35164 ; BAB35164 .
    GeneIDi 913110.
    960491.
    KEGGi ece:Z2016.
    ecs:ECs1741.
    PATRICi 18352746. VBIEscCol44059_1596.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-1725-MONOMER.
    ECOO157:ADHE-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiADHE_ECO57
    AccessioniPrimary (citable) accession number: P0A9Q8
    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 65 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, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3