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Reviewed, UniProtKB/Swiss-Prot P00334 (ADH_DROME)

Last modified November 25, 2008. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase
    EC=1.1.1.1
Gene names
Name: Adh
ORF Names: CG3481
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

An alcohol + NAD(+) = an aldehyde or ketone + NADH.

Enzyme regulation

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

Subunit structure

Homodimer.

Polymorphism

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.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords

   Coding sequence diversityPolymorphism
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processalcohol catabolic process Ref.27

Inferred from mutant phenotype. Source: UniProtKB

behavioral response to ethanol

Inferred from mutant phenotype. Source: FlyBase

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentlipid particle

Inferred from direct assay. Source: FlyBase

   Molecular functionalcohol dehydrogenase activity Ref.14 Ref.27

Inferred from mutant phenotype. Source: UniProtKB

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 256255Alcohol dehydrogenase
PRO_0000054474

Regions

Nucleotide binding12 – 4130NAD

Sites

Active site1531Proton acceptor
Binding site651NAD
Binding site1401Substrate
Binding site1571NAD

Amino acid modifications

Modified residue21N-acetylserine

Natural variations

Natural variant91N → V in allele Adh-UF.
Natural variant461A → D in allele Adh-UF.
Natural variant461A → V in strain: NC16.
Natural variant521A → E in allele Adh-F'.
Natural variant711A → S in strain: NC16.
Natural variant1931K → T in allele Adh-F, allele Adh-F-CHD, allele Adh-71K, allele Adh-JA-F and in strain Berkeley.
Natural variant2151P → S in allele Adh-F-CHD and allele Adh-71K.

Experimental info

Mutagenesis151G → A: 31% decrease in activity
Mutagenesis151G → D in Adh-N11; loss of activity
Mutagenesis151G → V: Complete loss of activity
Mutagenesis1301G → C: Complete loss of activity
Mutagenesis1331G → I: Complete loss of activity
Mutagenesis1361C → A: No decrease in activity
Mutagenesis1531Y → C: Retains only 0.25% activity
Mutagenesis1531Y → F, H, E or Q: Complete loss of activity
Mutagenesis1571K → I: Complete loss of activity
Mutagenesis1571K → R: Retains only 2.2% activity
Mutagenesis1841G → L: Complete loss of activity
Mutagenesis2191C → A: No decrease in activity

Secondary structure

.......................................... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00334-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EB4DF91029007284

FASTA25627,761
        10         20         30         40         50         60 
MSFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL KAINPKVTVT 

        70         80         90        100        110        120 
FYPYDVTVPI AETTKLLKTI FAQLKTVDVL INGAGILDDH QIERTIAVNY TGLVNTTTAI 

       130        140        150        160        170        180 
LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT 

       190        200        210        220        230        240 
VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL 

       250 
GTLEAIQWTK HWDSGI 

« Hide

References

« Hide 'large scale' references
[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: 6789320] [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: 6818527] [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: 6410283] [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: 3928896] [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: 3021568] [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: 3108863] [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: 3137352] [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: 2124644] [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: 1673107] [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: 1683848] [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: 7498745] [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: 10605124] [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. expand/collapse author list , 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: 10471707] [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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[16]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[17]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
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: 115502] [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: 6821373] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-256 (ALLELES ADH-F; ADH-S; ADH-UF AND AD