Reviewed,
UniProtKB/Swiss-Prot P00334 (ADH_DROME)
Last modified
November 25, 2008.
Version 114.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase EC=1.1.1.1 | ||||
| Gene names |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 256 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 diversity | Polymorphism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | alcohol catabolic process Ref.27 Inferred from mutant phenotype. Source: UniProtKB behavioral response to ethanolInferred from mutant phenotype. Source: FlyBase oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | lipid particle Inferred from direct assay. Source: FlyBase |
| Molecular function | alcohol dehydrogenase activity Ref.14 Ref.27 Inferred from mutant phenotype. Source: UniProtKB bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 256 | 255 | Alcohol dehydrogenase | PRO_0000054474 | ||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 12 – 41 | 30 | NAD | |||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 153 | 1 | Proton acceptor | |||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 65 | 1 | NAD | |||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 140 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 157 | 1 | NAD | |||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine | |||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 9 | 1 | N → V in allele Adh-UF. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 46 | 1 | A → D in allele Adh-UF. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 46 | 1 | A → V in strain: NC16. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 52 | 1 | A → E in allele Adh-F'. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 71 | 1 | A → S in strain: NC16. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 193 | 1 | K → T in allele Adh-F, allele Adh-F-CHD, allele Adh-71K, allele Adh-JA-F and in strain Berkeley. | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 215 | 1 | P → S in allele Adh-F-CHD and allele Adh-71K. | |||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 15 | 1 | G → A: 31% decrease in activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 15 | 1 | G → D in Adh-N11; loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 15 | 1 | G → V: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 130 | 1 | G → C: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 133 | 1 | G → I: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 136 | 1 | C → A: No decrease in activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 153 | 1 | Y → C: Retains only 0.25% activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 153 | 1 | Y → F, H, E or Q: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 157 | 1 | K → I: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 157 | 1 | K → R: Retains only 2.2% activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 184 | 1 | G → L: Complete loss of activity | |||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 219 | 1 | C → A: No decrease in activity | |||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 9 – 13 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 14 – 16 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 27 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 40 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 44 – 53 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 57 – 63 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 70 – 84 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 89 – 92 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 102 – 109 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 124 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 126 – 128 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 138 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 141 – 143 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 151 – 174 | 24 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 175 – 183 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 185 – 188 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 189 – 192 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 197 – 199 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 204 – 209 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 216 – 229 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 235 – 239 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 242 – 245 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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. 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 |

Clusters with