ADH_DROME
ID ADH_DROME Reviewed; 256 AA.
AC P00334; A4V0Q1; Q27332; Q27579; Q27596; Q2MGK2; Q53XD5; Q95TC8; Q9NKC0;
AC Q9VJS3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh; ORFNames=CG3481;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
RX PubMed=6789320; DOI=10.1073/pnas.78.5.2717;
RA Benyajati C., Place A.R., Powers D.A., Sofer W.;
RT "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of
RT intervening sequences to functional domains in the protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2717-2721(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
RX PubMed=6818527; DOI=10.1093/nar/10.22.7145;
RA Kubli E., Schmidt T., Martin P.F., Sofer W.;
RT "In vitro suppression of a nonsense mutant of Drosophila melanogaster.";
RL Nucleic Acids Res. 10:7145-7152(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-S AND ADH-F).
RX PubMed=6410283; DOI=10.1038/304412a0;
RA Kreitman M.;
RT "Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila
RT melanogaster.";
RL Nature 304:412-417(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
RX PubMed=3928896; DOI=10.1016/0022-2836(85)90375-4;
RA Martin P.F., Place A.R., Pentz E., Sofer W.;
RT "UGA nonsense mutation in the alcohol dehydrogenase gene of Drosophila
RT melanogaster.";
RL J. Mol. Biol. 184:221-229(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-JA-F AND ADH-AF-S).
RX PubMed=3021568; DOI=10.1093/genetics/114.1.93;
RA Kreitman M.E., Aguade M.;
RT "Excess polymorphism at the Adh locus in Drosophila melanogaster.";
RL Genetics 114:93-110(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-N4).
RX PubMed=3108863; DOI=10.1093/nar/15.9.3931;
RA Chia W., Savakis C., Karp R., Ashburner M.;
RT "Adhn4 of Drosophila melanogaster is a nonsense mutation.";
RL Nucleic Acids Res. 15:3931-3931(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F-CHD).
RC TISSUE=Embryo;
RX PubMed=3137352; DOI=10.1007/bf02138374;
RA Collet C.;
RT "Recent origin for a thermostable alcohol dehydrogenase allele of
RT Drosophila melanogaster.";
RL J. Mol. Evol. 27:142-146(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-71K).
RX PubMed=2124644; DOI=10.1093/oxfordjournals.molbev.a040614;
RA Eisses K.T., Andriesse A.J., de Boer A.D., Thorig G.E.W., Weisbeek P.J.;
RT "Analysis of the gene encoding the multifunctional alcohol dehydrogenase
RT allozyme ADH-71k of Drosophila melanogaster.";
RL Mol. Biol. Evol. 7:459-469(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
RX PubMed=1673107; DOI=10.1093/genetics/127.3.565;
RA Kreitman M., Hudson R.R.;
RT "Inferring the evolutionary histories of the Adh and Adh-dup loci in
RT Drosophila melanogaster from patterns of polymorphism and divergence.";
RL Genetics 127:565-582(1991).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F).
RC STRAIN=KA12, NC-016, and RI32;
RX PubMed=1683848; DOI=10.1093/genetics/129.2.489;
RA Laurie C.C., Bridgham J.T., Choudhary M.;
RT "Associations between DNA sequence variation and variation in expression of
RT the Adh gene in natural populations of Drosophila melanogaster.";
RL Genetics 129:489-499(1991).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7498745; DOI=10.1093/genetics/140.2.667;
RA Dunn R.C., Laurie C.C.;
RT "Effects of a transposable element insertion on alcohol dehydrogenase
RT expression in Drosophila melanogaster.";
RL Genetics 140:667-677(1995).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE ADH-S).
RC STRAIN=Canton-S;
RA Brogna S., Ashburner M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-H3; ADH-H12; ADH-H13;
RP ADH-H18; ADH-H21; ADH-K15; ADH-K30; ADH-K35; ADH-K37 AND ADH-K82).
RC STRAIN=Zimbabwe;
RX PubMed=10605124; DOI=10.1093/oxfordjournals.molbev.a026095;
RA Begun D., Betancourt A., Langley C., Stephan W.;
RT "Is the fast/slow allozyme variation at the Adh locus of Drosophila
RT melanogaster an ancient balanced polymorphism?";
RL Mol. Biol. Evol. 16:1816-1819(1999).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [16]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [18]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [19]
RP PROTEIN SEQUENCE OF 2-256 (ALLELE ADH-F').
RX PubMed=115502; DOI=10.1016/s0300-9084(79)80169-8;
RA Retzios A.D., Thatcher D.R.;
RT "Chemical basis of the electrophoretic variation observed at the alcohol
RT dehydrogenase locus of Drosophila melanogaster.";
RL Biochimie 61:701-704(1979).
RN [20]
RP PROTEIN SEQUENCE OF 2-256 (ALLELES ADH-F; ADH-S; ADH-UF AND ADH-N11), AND
RP ACETYLATION AT SER-2.
RX PubMed=6821373; DOI=10.1042/bj1870875;
RA Thatcher D.R.;
RT "The complete amino acid sequence of three alcohol dehydrogenase
RT alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila
RT melanogaster.";
RL Biochem. J. 187:875-883(1980).
RN [21]
RP ERRATUM OF PUBMED:6821373.
RA Thatcher D.R.;
RL Biochem. J. 191:895-895(1980).
RN [22]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-256 (ALLELE ADH-NLA248).
RX PubMed=2419573; DOI=10.1016/0022-2836(85)90388-2;
RA Chia W., Savakis C., Karp R., Pelham H., Ashburner M.;
RT "Mutation of the Adh gene of Drosophila melanogaster containing an internal
RT tandem duplication.";
RL J. Mol. Biol. 186:679-688(1985).
RN [23]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-256 (ALLELE ADH-F).
RX PubMed=6780981; DOI=10.1093/nar/8.23.5649;
RA Benyajati C., Wang N., Reddy A., Weinberg E., Sofer W.;
RT "Alcohol dehydrogenase in Drosophila: isolation and characterization of
RT messenger RNA and cDNA clone.";
RL Nucleic Acids Res. 8:5649-5667(1980).
RN [24]
RP PROTEIN SEQUENCE OF 208-225 (ALLELE ADH-F-CHD).
RX PubMed=6789328; DOI=10.1073/pnas.78.5.3103;
RA Chambers G.K., Laver W.G., Campbell S., Gibson J.B.;
RT "Structural analysis of an electrophoretically cryptic alcohol
RT dehydrogenase variant from an Australian population of Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:3103-3107(1981).
RN [25]
RP MUTAGENESIS.
RX PubMed=2108721; DOI=10.1021/bi00457a003;
RA Chen Z., Lu L., Shirley M., Lee W.R., Chang S.H.;
RT "Site-directed mutagenesis of glycine-14 and two 'critical' cysteinyl
RT residues in Drosophila alcohol dehydrogenase.";
RL Biochemistry 29:1112-1118(1990).
RN [26]
RP MUTAGENESIS OF TYR-153.
RX PubMed=1505661; DOI=10.1016/0014-5793(92)81282-q;
RA Albalat R., Gonzalez-Duarte R., Atrian S.;
RT "Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl
RT group of Tyr152 is involved in the active site of the enzyme.";
RL FEBS Lett. 308:235-239(1992).
RN [27]
RP MUTAGENESIS OF TYR-153 AND LYS-157.
RX PubMed=8461298; DOI=10.1021/bi00064a017;
RA Chen Z., Jiang J.C., Lin Z.-G., Lee W.R., Baker M.E., Chang S.H.;
RT "Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence
RT for involvement of tyrosine-152 and lysine-156 in catalysis.";
RL Biochemistry 32:3342-3346(1993).
RN [28]
RP MUTAGENESIS OF GLY-130; GLY-133; TYR-153; LYS-157 AND GLY-184.
RX PubMed=8454065; DOI=10.1016/0014-5793(93)80043-t;
RA Cols N., Marfany G., Atrian S., Gonzalez-Duarte R.;
RT "Effect of site-directed mutagenesis on conserved positions of Drosophila
RT alcohol dehydrogenase.";
RL FEBS Lett. 319:90-94(1993).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
RX PubMed=15581900; DOI=10.1016/j.jmb.2004.10.028;
RA Benach J., Winberg J.-O., Svendsen J.-S., Atrian S., Gonzalez-Duarte R.,
RA Ladenstein R.;
RT "Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel
RT insights into the effects of electrostatics on catalysis.";
RL J. Mol. Biol. 345:579-598(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- ACTIVITY REGULATION: Inhibited by 2,2,2-trifluoroethanol and pyrazole.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15581900}.
CC -!- POLYMORPHISM: Virtually all natural populations of this species are
CC polymorphic for 2 electrophoretically distinguishable alleles, Adh-S
CC and Adh-F (PubMed:6789320, PubMed:6410283, PubMed:1673107,
CC PubMed:1683848, Ref.12, PubMed:12537569, Ref.18, PubMed:6821373,
CC PubMed:6780981). The sequence of the Adh-S allele is shown
CC (PubMed:6789320, PubMed:6410283, PubMed:1673107, Ref.12,
CC PubMed:12537569, Ref.18, PubMed:6821373). Other naturally occurring
CC alleles include Adh-JA-F, Adh-AF-S, Adh-F-CHD, Adh-71K, Adh-UF and Adh-
CC F' (PubMed:3021568, PubMed:3137352, PubMed:2124644, PubMed:6789328,
CC PubMed:115502, PubMed:6821373). Artificially induced mutations include
CC Adh-NB, Adh-NLA248, Adh-N4 and Adh-N11 (PubMed:6818527, PubMed:3928896,
CC PubMed:3108863, PubMed:6821373, PubMed:2419573).
CC {ECO:0000269|PubMed:115502, ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:1673107, ECO:0000269|PubMed:1683848,
CC ECO:0000269|PubMed:2124644, ECO:0000269|PubMed:2419573,
CC ECO:0000269|PubMed:3021568, ECO:0000269|PubMed:3108863,
CC ECO:0000269|PubMed:3137352, ECO:0000269|PubMed:3928896,
CC ECO:0000269|PubMed:6410283, ECO:0000269|PubMed:6780981,
CC ECO:0000269|PubMed:6789320, ECO:0000269|PubMed:6789328,
CC ECO:0000269|PubMed:6818527, ECO:0000269|PubMed:6821373,
CC ECO:0000269|Ref.12, ECO:0000269|Ref.18}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; M17827; AAA28341.1; -; Genomic_DNA.
DR EMBL; M17828; AAA28342.1; -; Genomic_DNA.
DR EMBL; M19547; AAA70210.1; -; Genomic_DNA.
DR EMBL; M17830; AAA28343.1; -; Genomic_DNA.
DR EMBL; M17831; AAA28344.1; -; Genomic_DNA.
DR EMBL; M17832; AAA28345.1; -; Genomic_DNA.
DR EMBL; M17833; AAA28346.1; -; Genomic_DNA.
DR EMBL; M17834; AAA28347.1; -; Genomic_DNA.
DR EMBL; M17835; AAA28348.1; -; Genomic_DNA.
DR EMBL; M17836; AAA28349.1; -; Genomic_DNA.
DR EMBL; M17837; AAA70212.1; -; Genomic_DNA.
DR EMBL; Z00030; CAA77330.1; -; Genomic_DNA.
DR EMBL; M22210; AAA28338.1; -; Genomic_DNA.
DR EMBL; M57239; AAA28330.1; -; Genomic_DNA.
DR EMBL; X78384; CAA55151.1; -; Genomic_DNA.
DR EMBL; M36580; AAA28331.1; -; Genomic_DNA.
DR EMBL; X60791; CAA43204.1; -; Genomic_DNA.
DR EMBL; X60792; CAA43205.1; -; Genomic_DNA.
DR EMBL; X60793; CAA43206.1; -; Genomic_DNA.
DR EMBL; U20765; AAA88817.1; -; Genomic_DNA.
DR EMBL; X98338; CAA66981.1; -; mRNA.
DR EMBL; AF175211; AAF00229.1; -; Genomic_DNA.
DR EMBL; AF175212; AAF00230.1; -; Genomic_DNA.
DR EMBL; AF175213; AAF00231.1; -; Genomic_DNA.
DR EMBL; AF175214; AAF00232.1; -; Genomic_DNA.
DR EMBL; AF175215; AAF00233.1; -; Genomic_DNA.
DR EMBL; AF175216; AAF00234.1; -; Genomic_DNA.
DR EMBL; AF175217; AAF00235.1; -; Genomic_DNA.
DR EMBL; AF175218; AAF00236.1; -; Genomic_DNA.
DR EMBL; AF175219; AAF00237.1; -; Genomic_DNA.
DR EMBL; AF175220; AAF00238.1; -; Genomic_DNA.
DR EMBL; AE014134; AAO41197.1; -; Genomic_DNA.
DR EMBL; AE014134; AAO41199.1; -; Genomic_DNA.
DR EMBL; AE014134; AAO41200.1; -; Genomic_DNA.
DR EMBL; AE014134; AAO41201.1; -; Genomic_DNA.
DR EMBL; AY060227; AAL25266.1; -; mRNA.
DR EMBL; BT012435; AAS93706.1; -; mRNA.
DR EMBL; M17845; AAA28363.1; -; Genomic_DNA.
DR PIR; A93309; DEFFA.
DR RefSeq; NP_001027266.1; NM_001032095.2.
DR RefSeq; NP_001027267.1; NM_001032096.2.
DR RefSeq; NP_001027268.1; NM_001032097.2.
DR RefSeq; NP_001027269.1; NM_001032098.2.
DR RefSeq; NP_001027270.1; NM_001032099.2.
DR PDB; 1MG5; X-ray; 1.63 A; A/B=2-256.
DR PDBsum; 1MG5; -.
DR AlphaFoldDB; P00334; -.
DR SMR; P00334; -.
DR BioGRID; 533474; 61.
DR IntAct; P00334; 19.
DR STRING; 7227.FBpp0100048; -.
DR iPTMnet; P00334; -.
DR PaxDb; P00334; -.
DR PeptideAtlas; P00334; -.
DR PRIDE; P00334; -.
DR DNASU; 3771877; -.
DR EnsemblMetazoa; FBtr0100589; FBpp0100045; FBgn0000055.
DR EnsemblMetazoa; FBtr0100590; FBpp0100047; FBgn0000055.
DR EnsemblMetazoa; FBtr0100591; FBpp0100048; FBgn0000055.
DR EnsemblMetazoa; FBtr0100593; FBpp0100050; FBgn0000055.
DR EnsemblMetazoa; FBtr0100594; FBpp0100051; FBgn0000055.
DR GeneID; 3771877; -.
DR KEGG; dme:Dmel_CG3481; -.
DR CTD; 3771877; -.
DR FlyBase; FBgn0000055; Adh.
DR VEuPathDB; VectorBase:FBgn0000055; -.
DR eggNOG; KOG4169; Eukaryota.
DR GeneTree; ENSGT00940000154593; -.
DR HOGENOM; CLU_010194_2_16_1; -.
DR InParanoid; P00334; -.
DR PhylomeDB; P00334; -.
DR SABIO-RK; P00334; -.
DR SignaLink; P00334; -.
DR BioGRID-ORCS; 3771877; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Adh; fly.
DR EvolutionaryTrace; P00334; -.
DR GenomeRNAi; 3771877; -.
DR PRO; PR:P00334; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000055; Expressed in insect adult head and 32 other tissues.
DR ExpressionAtlas; P00334; baseline and differential.
DR Genevisible; P00334; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:FlyBase.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:FlyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0006117; P:acetaldehyde metabolic process; IDA:FlyBase.
DR GO; GO:0046164; P:alcohol catabolic process; IMP:UniProtKB.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0006067; P:ethanol metabolic process; IMP:FlyBase.
DR GO; GO:0006069; P:ethanol oxidation; IDA:FlyBase.
DR GO; GO:0006734; P:NADH metabolic process; IDA:FlyBase.
DR InterPro; IPR002425; ADH_Drosophila-type.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR01168; ALCDHDRGNASE.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:115502,
FT ECO:0000269|PubMed:6821373"
FT CHAIN 2..256
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000054474"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15581900"
FT BINDING 12..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15581900"
FT BINDING 65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15581900"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15581900"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15581900"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6821373"
FT VARIANT 9
FT /note="N -> V (in allele Adh-UF)"
FT VARIANT 46
FT /note="A -> D (in allele Adh-UF)"
FT VARIANT 46
FT /note="A -> V (in strain: NC16)"
FT VARIANT 52
FT /note="A -> E (in allele Adh-F')"
FT VARIANT 71
FT /note="A -> S (in strain: NC16)"
FT VARIANT 193
FT /note="K -> T (in allele Adh-F, allele Adh-F-CHD, allele
FT Adh-71K, allele Adh-JA-F and in strain: Berkeley)"
FT VARIANT 215
FT /note="P -> S (in allele Adh-F-CHD and allele Adh-71K)"
FT MUTAGEN 15
FT /note="G->A: 31% decrease in activity."
FT /evidence="ECO:0000269|PubMed:2108721"
FT MUTAGEN 15
FT /note="G->D: In Adh-N11; loss of activity."
FT /evidence="ECO:0000269|PubMed:2108721"
FT MUTAGEN 15
FT /note="G->V: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:2108721"
FT MUTAGEN 130
FT /note="G->C: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8454065"
FT MUTAGEN 133
FT /note="G->I: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8454065"
FT MUTAGEN 136
FT /note="C->A: No decrease in activity."
FT /evidence="ECO:0000269|PubMed:2108721"
FT MUTAGEN 153
FT /note="Y->C: Retains only 0.25% activity."
FT /evidence="ECO:0000269|PubMed:1505661,
FT ECO:0000269|PubMed:8454065, ECO:0000269|PubMed:8461298"
FT MUTAGEN 153
FT /note="Y->F,H,E,Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1505661,
FT ECO:0000269|PubMed:8454065, ECO:0000269|PubMed:8461298"
FT MUTAGEN 157
FT /note="K->I: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8454065,
FT ECO:0000269|PubMed:8461298"
FT MUTAGEN 157
FT /note="K->R: Retains only 2.2% activity."
FT /evidence="ECO:0000269|PubMed:8454065,
FT ECO:0000269|PubMed:8461298"
FT MUTAGEN 184
FT /note="G->L: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8454065"
FT MUTAGEN 219
FT /note="C->A: No decrease in activity."
FT /evidence="ECO:0000269|PubMed:2108721"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1MG5"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 151..174
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1MG5"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:1MG5"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1MG5"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1MG5"
SQ SEQUENCE 256 AA; 27761 MW; EB4DF91029007284 CRC64;
MSFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL KAINPKVTVT
FYPYDVTVPI AETTKLLKTI FAQLKTVDVL INGAGILDDH QIERTIAVNY TGLVNTTTAI
LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT
VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL
GTLEAIQWTK HWDSGI
