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P00334

- ADH_DROME

UniProt

P00334 - ADH_DROME

Protein

Alcohol dehydrogenase

Gene

Adh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    An alcohol + NAD+ = an aldehyde or ketone + NADH.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by 2,2,2-trifluoroethanol and pyrazole.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651NAD1 Publication
    Binding sitei140 – 1401Substrate1 Publication
    Active sitei153 – 1531Proton acceptor
    Binding sitei157 – 1571NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 4130NAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: UniProtKB
    2. protein homodimerization activity Source: FlyBase

    GO - Biological processi

    1. alcohol catabolic process Source: UniProtKB
    2. alcohol metabolic process Source: FlyBase
    3. behavioral response to ethanol Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_184367. Synthesis of Lipoxins (LX).
    REACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RKP00334.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase (EC:1.1.1.1)
    Gene namesi
    Name:Adh
    ORF Names:CG3481
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0000055. Adh.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: FlyBase
    2. lipid particle Source: FlyBase
    3. microtubule associated complex Source: FlyBase
    4. protein complex Source: FlyBase

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151G → A: 31% decrease in activity. 1 Publication
    Mutagenesisi15 – 151G → D in Adh-N11; loss of activity. 1 Publication
    Mutagenesisi15 – 151G → V: Complete loss of activity. 1 Publication
    Mutagenesisi130 – 1301G → C: Complete loss of activity. 2 Publications
    Mutagenesisi133 – 1331G → I: Complete loss of activity. 2 Publications
    Mutagenesisi136 – 1361C → A: No decrease in activity. 1 Publication
    Mutagenesisi153 – 1531Y → C: Retains only 0.25% activity. 4 Publications
    Mutagenesisi153 – 1531Y → F, H, E or Q: Complete loss of activity. 4 Publications
    Mutagenesisi157 – 1571K → I: Complete loss of activity. 3 Publications
    Mutagenesisi157 – 1571K → R: Retains only 2.2% activity. 3 Publications
    Mutagenesisi184 – 1841G → L: Complete loss of activity. 2 Publications
    Mutagenesisi219 – 2191C → A: No decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 256255Alcohol dehydrogenasePRO_0000054474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00334.
    PRIDEiP00334.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi533474. 58 interactions.
    IntActiP00334. 1 interaction.
    MINTiMINT-877153.

    Structurei

    Secondary structure

    1
    256
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Turni14 – 163
    Helixi18 – 2710
    Beta strandi33 – 408
    Helixi44 – 5310
    Beta strandi57 – 637
    Helixi70 – 8415
    Beta strandi89 – 924
    Helixi102 – 1098
    Helixi111 – 12414
    Helixi126 – 1283
    Beta strandi133 – 1386
    Helixi141 – 1433
    Helixi151 – 17424
    Beta strandi175 – 1839
    Beta strandi185 – 1884
    Turni189 – 1924
    Helixi197 – 1993
    Helixi204 – 2096
    Helixi216 – 22914
    Beta strandi235 – 2395
    Beta strandi242 – 2454

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MG5X-ray1.63A/B2-256[»]
    ProteinModelPortaliP00334.
    SMRiP00334. Positions 2-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00334.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    InParanoidiP00334.
    KOiK00001.
    OrthoDBiEOG7966HT.
    PhylomeDBiP00334.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002425. ADH_Drosophila-type.
    IPR002424. ADH_insect.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR01168. ALCDHDRGNASE.
    PR01167. INSADHFAMILY.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00334-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL    50
    KAINPKVTVT FYPYDVTVPI AETTKLLKTI FAQLKTVDVL INGAGILDDH 100
    QIERTIAVNY TGLVNTTTAI LDFWDKRKGG PGGIICNIGS VTGFNAIYQV 150
    PVYSGTKAAV VNFTSSLAKL APITGVTAYT VNPGITRTTL VHKFNSWLDV 200
    EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL GTLEAIQWTK 250
    HWDSGI 256
    Length:256
    Mass (Da):27,761
    Last modified:January 23, 2007 - v2
    Checksum:iEB4DF91029007284
    GO

    Polymorphismi

    Virtually all natural populations of this species are polymorphic for 2 electrophoretically distinguishable alleles, Adh-S and Adh-F. The sequence of the Adh-S allele is shown. Other naturally occurring alleles include Adh-JA-F, Adh-AF-S, Adh-F-CHD, Adh-71K, Adh-UF and Adh-F'. Artificially induced mutations include Adh-NB, Adh-NLA248, Adh-N4 and Adh-N11.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91N → V in allele Adh-UF.
    Natural varianti46 – 461A → D in allele Adh-UF.
    Natural varianti46 – 461A → V in strain: NC16.
    Natural varianti52 – 521A → E in allele Adh-F'.
    Natural varianti71 – 711A → S in strain: NC16.
    Natural varianti193 – 1931K → T in allele Adh-F, allele Adh-F-CHD, allele Adh-71K, allele Adh-JA-F and in strain Berkeley.
    Natural varianti215 – 2151P → S in allele Adh-F-CHD and allele Adh-71K.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17827 Genomic DNA. Translation: AAA28341.1.
    M17828 Genomic DNA. Translation: AAA28342.1.
    M19547 Genomic DNA. Translation: AAA70210.1.
    M17830 Genomic DNA. Translation: AAA28343.1.
    M17831 Genomic DNA. Translation: AAA28344.1.
    M17832 Genomic DNA. Translation: AAA28345.1.
    M17833 Genomic DNA. Translation: AAA28346.1.
    M17834 Genomic DNA. Translation: AAA28347.1.
    M17835 Genomic DNA. Translation: AAA28348.1.
    M17836 Genomic DNA. Translation: AAA28349.1.
    M17837 Genomic DNA. Translation: AAA70212.1.
    Z00030 Genomic DNA. Translation: CAA77330.1.
    M22210 Genomic DNA. Translation: AAA28338.1.
    M57239 Genomic DNA. Translation: AAA28330.1.
    X78384 Genomic DNA. Translation: CAA55151.1.
    M36580 Genomic DNA. Translation: AAA28331.1.
    X60791 Genomic DNA. Translation: CAA43204.1.
    X60792 Genomic DNA. Translation: CAA43205.1.
    X60793 Genomic DNA. Translation: CAA43206.1.
    U20765 Genomic DNA. Translation: AAA88817.1.
    X98338 mRNA. Translation: CAA66981.1.
    AF175211 Genomic DNA. Translation: AAF00229.1.
    AF175212 Genomic DNA. Translation: AAF00230.1.
    AF175213 Genomic DNA. Translation: AAF00231.1.
    AF175214 Genomic DNA. Translation: AAF00232.1.
    AF175215 Genomic DNA. Translation: AAF00233.1.
    AF175216 Genomic DNA. Translation: AAF00234.1.
    AF175217 Genomic DNA. Translation: AAF00235.1.
    AF175218 Genomic DNA. Translation: AAF00236.1.
    AF175219 Genomic DNA. Translation: AAF00237.1.
    AF175220 Genomic DNA. Translation: AAF00238.1.
    AE014134 Genomic DNA. Translation: AAO41197.1.
    AE014134 Genomic DNA. Translation: AAO41199.1.
    AE014134 Genomic DNA. Translation: AAO41200.1.
    AE014134 Genomic DNA. Translation: AAO41201.1.
    AY060227 mRNA. Translation: AAL25266.1.
    BT012435 mRNA. Translation: AAS93706.1.
    M17845 Genomic DNA. Translation: AAA28363.1.
    PIRiA93309. DEFFA.
    RefSeqiNP_001027266.1. NM_001032095.1.
    NP_001027267.1. NM_001032096.1.
    NP_001027268.1. NM_001032097.1.
    NP_001027269.1. NM_001032098.1.
    NP_001027270.1. NM_001032099.1.
    UniGeneiDm.6818.

    Genome annotation databases

    GeneIDi3771877.
    KEGGidme:Dmel_CG3481.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17827 Genomic DNA. Translation: AAA28341.1 .
    M17828 Genomic DNA. Translation: AAA28342.1 .
    M19547 Genomic DNA. Translation: AAA70210.1 .
    M17830 Genomic DNA. Translation: AAA28343.1 .
    M17831 Genomic DNA. Translation: AAA28344.1 .
    M17832 Genomic DNA. Translation: AAA28345.1 .
    M17833 Genomic DNA. Translation: AAA28346.1 .
    M17834 Genomic DNA. Translation: AAA28347.1 .
    M17835 Genomic DNA. Translation: AAA28348.1 .
    M17836 Genomic DNA. Translation: AAA28349.1 .
    M17837 Genomic DNA. Translation: AAA70212.1 .
    Z00030 Genomic DNA. Translation: CAA77330.1 .
    M22210 Genomic DNA. Translation: AAA28338.1 .
    M57239 Genomic DNA. Translation: AAA28330.1 .
    X78384 Genomic DNA. Translation: CAA55151.1 .
    M36580 Genomic DNA. Translation: AAA28331.1 .
    X60791 Genomic DNA. Translation: CAA43204.1 .
    X60792 Genomic DNA. Translation: CAA43205.1 .
    X60793 Genomic DNA. Translation: CAA43206.1 .
    U20765 Genomic DNA. Translation: AAA88817.1 .
    X98338 mRNA. Translation: CAA66981.1 .
    AF175211 Genomic DNA. Translation: AAF00229.1 .
    AF175212 Genomic DNA. Translation: AAF00230.1 .
    AF175213 Genomic DNA. Translation: AAF00231.1 .
    AF175214 Genomic DNA. Translation: AAF00232.1 .
    AF175215 Genomic DNA. Translation: AAF00233.1 .
    AF175216 Genomic DNA. Translation: AAF00234.1 .
    AF175217 Genomic DNA. Translation: AAF00235.1 .
    AF175218 Genomic DNA. Translation: AAF00236.1 .
    AF175219 Genomic DNA. Translation: AAF00237.1 .
    AF175220 Genomic DNA. Translation: AAF00238.1 .
    AE014134 Genomic DNA. Translation: AAO41197.1 .
    AE014134 Genomic DNA. Translation: AAO41199.1 .
    AE014134 Genomic DNA. Translation: AAO41200.1 .
    AE014134 Genomic DNA. Translation: AAO41201.1 .
    AY060227 mRNA. Translation: AAL25266.1 .
    BT012435 mRNA. Translation: AAS93706.1 .
    M17845 Genomic DNA. Translation: AAA28363.1 .
    PIRi A93309. DEFFA.
    RefSeqi NP_001027266.1. NM_001032095.1.
    NP_001027267.1. NM_001032096.1.
    NP_001027268.1. NM_001032097.1.
    NP_001027269.1. NM_001032098.1.
    NP_001027270.1. NM_001032099.1.
    UniGenei Dm.6818.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MG5 X-ray 1.63 A/B 2-256 [» ]
    ProteinModelPortali P00334.
    SMRi P00334. Positions 2-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 533474. 58 interactions.
    IntActi P00334. 1 interaction.
    MINTi MINT-877153.

    Proteomic databases

    PaxDbi P00334.
    PRIDEi P00334.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3771877.
    KEGGi dme:Dmel_CG3481.

    Organism-specific databases

    CTDi 3771877.
    FlyBasei FBgn0000055. Adh.

    Phylogenomic databases

    eggNOGi COG1028.
    InParanoidi P00334.
    KOi K00001.
    OrthoDBi EOG7966HT.
    PhylomeDBi P00334.

    Enzyme and pathway databases

    Reactomei REACT_184367. Synthesis of Lipoxins (LX).
    REACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RK P00334.

    Miscellaneous databases

    EvolutionaryTracei P00334.
    GenomeRNAii 3771877.
    NextBioi 851589.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002425. ADH_Drosophila-type.
    IPR002424. ADH_insect.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR01168. ALCDHDRGNASE.
    PR01167. INSADHFAMILY.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein."
      Benyajati C., Place A.R., Powers D.A., Sofer W.
      Proc. Natl. Acad. Sci. U.S.A. 78:2717-2721(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
    2. "In vitro suppression of a nonsense mutant of Drosophila melanogaster."
      Kubli E., Schmidt T., Martin P.F., Sofer W.
      Nucleic Acids Res. 10:7145-7152(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
    3. "Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster."
      Kreitman M.
      Nature 304:412-417(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-S AND ADH-F).
    4. "UGA nonsense mutation in the alcohol dehydrogenase gene of Drosophila melanogaster."
      Martin P.F., Place A.R., Pentz E., Sofer W.
      J. Mol. Biol. 184:221-229(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
    5. "Excess polymorphism at the Adh locus in Drosophila melanogaster."
      Kreitman M.E., Aguade M.
      Genetics 114:93-110(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-JA-F AND ADH-AF-S).
    6. "Adhn4 of Drosophila melanogaster is a nonsense mutation."
      Chia W., Savakis C., Karp R., Ashburner M.
      Nucleic Acids Res. 15:3931-3931(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-N4).
    7. "Recent origin for a thermostable alcohol dehydrogenase allele of Drosophila melanogaster."
      Collet C.
      J. Mol. Evol. 27:142-146(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F-CHD).
      Tissue: Embryo.
    8. "Analysis of the gene encoding the multifunctional alcohol dehydrogenase allozyme ADH-71k of Drosophila melanogaster."
      Eisses K.T., Andriesse A.J., de Boer A.D., Thorig G.E.W., Weisbeek P.J.
      Mol. Biol. Evol. 7:459-469(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-71K).
    9. "Inferring the evolutionary histories of the Adh and Adh-dup loci in Drosophila melanogaster from patterns of polymorphism and divergence."
      Kreitman M., Hudson R.R.
      Genetics 127:565-582(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
    10. "Associations between DNA sequence variation and variation in expression of the Adh gene in natural populations of Drosophila melanogaster."
      Laurie C.C., Bridgham J.T., Choudhary M.
      Genetics 129:489-499(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F).
      Strain: KA12, NC-016 and RI32.
    11. "Effects of a transposable element insertion on alcohol dehydrogenase expression in Drosophila melanogaster."
      Dunn R.C., Laurie C.C.
      Genetics 140:667-677(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    12. Brogna S., Ashburner M.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE ADH-S).
      Strain: Canton-S.
    13. "Is the fast/slow allozyme variation at the Adh locus of Drosophila melanogaster an ancient balanced polymorphism?"
      Begun D., Betancourt A., Langley C., Stephan W.
      Mol. Biol. Evol. 16:1816-1819(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-H3; ADH-H12; ADH-H13; ADH-H18; ADH-H21; ADH-K15; ADH-K30; ADH-K35; ADH-K37 AND ADH-K82).
      Strain: Zimbabwe.
    14. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
      Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
      , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
      Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    15. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    16. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    17. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
      Strain: Berkeley.
      Tissue: Head.
    18. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
      Strain: Berkeley.
      Tissue: Head.
    19. "Chemical basis of the electrophoretic variation observed at the alcohol dehydrogenase locus of Drosophila melanogaster."
      Retzios A.D., Thatcher D.R.
      Biochimie 61:701-704(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-256 (ALLELE ADH-F').
    20. "The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster."
      Thatcher D.R.
      Biochem. J. 187:875-883(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-256 (ALLELES ADH-F; ADH-S; ADH-UF AND ADH-N11), ACETYLATION AT SER-2.
    21. Erratum
      Thatcher D.R.
      Biochem. J. 191:895-895(1980)
    22. "Mutation of the Adh gene of Drosophila melanogaster containing an internal tandem duplication."
      Chia W., Savakis C., Karp R., Pelham H., Ashburner M.
      J. Mol. Biol. 186:679-688(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-256 (ALLELE ADH-NLA248).
    23. "Alcohol dehydrogenase in Drosophila: isolation and characterization of messenger RNA and cDNA clone."
      Benyajati C., Wang N., Reddy A., Weinberg E., Sofer W.
      Nucleic Acids Res. 8:5649-5667(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-256 (ALLELE ADH-F).
    24. "Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster."
      Chambers G.K., Laver W.G., Campbell S., Gibson J.B.
      Proc. Natl. Acad. Sci. U.S.A. 78:3103-3107(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 208-225 (ALLELE ADH-F-CHD).
    25. "Site-directed mutagenesis of glycine-14 and two 'critical' cysteinyl residues in Drosophila alcohol dehydrogenase."
      Chen Z., Lu L., Shirley M., Lee W.R., Chang S.H.
      Biochemistry 29:1112-1118(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    26. "Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme."
      Albalat R., Gonzalez-Duarte R., Atrian S.
      FEBS Lett. 308:235-239(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-153.
    27. "Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis."
      Chen Z., Jiang J.C., Lin Z.-G., Lee W.R., Baker M.E., Chang S.H.
      Biochemistry 32:3342-3346(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-153 AND LYS-157.
    28. "Effect of site-directed mutagenesis on conserved positions of Drosophila alcohol dehydrogenase."
      Cols N., Marfany G., Atrian S., Gonzalez-Duarte R.
      FEBS Lett. 319:90-94(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-130; GLY-133; TYR-153; LYS-157 AND GLY-184.
    29. "Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis."
      Benach J., Winberg J.-O., Svendsen J.-S., Atrian S., Gonzalez-Duarte R., Ladenstein R.
      J. Mol. Biol. 345:579-598(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.

    Entry informationi

    Entry nameiADH_DROME
    AccessioniPrimary (citable) accession number: P00334
    Secondary accession number(s): A4V0Q1
    , Q27332, Q27579, Q27596, Q2MGK2, Q53XD5, Q95TC8, Q9NKC0, Q9VJS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3