P00334 (ADH_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase
EC=1.1.1.1

Gene names

Name:	Adh
ORF Names:	CG3481

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

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 Reference proteome
Gene Ontology (GO)
Biological_process	alcohol catabolic process Inferred from mutant phenotype Ref.27. Source: UniProtKB behavioral response to ethanol Inferred from mutant phenotype PubMed 12486199. Source: FlyBase
Cellular_component	cytosol Inferred from direct assay PubMed 8353517. Source: FlyBase lipid particle Inferred from direct assay PubMed 16543254. Source: FlyBase microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase
Molecular_function	alcohol dehydrogenase (NAD) activity Inferred from mutant phenotype Ref.27. Source: UniProtKB nucleotide binding Inferred 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 Ref.19 Ref.20

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 Ref.20

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. Ref.28

Mutagenesis

133

1

G → I: Complete loss of activity. Ref.28

Mutagenesis

136

1

C → A: No decrease in activity.

Mutagenesis

153

1

Y → C: Retains only 0.25% activity. Ref.26 Ref.27 Ref.28

Mutagenesis

153

1

Y → F, H, E or Q: Complete loss of activity. Ref.26 Ref.27 Ref.28

Mutagenesis

157

1

K → I: Complete loss of activity. Ref.27 Ref.28

Mutagenesis

157

1

K → R: Retains only 2.2% activity. Ref.27 Ref.28

Mutagenesis

184

1

G → L: Complete loss of activity. Ref.28

Mutagenesis

219

1

C → A: No decrease in activity.

Secondary structure

1

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256

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P00334 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EB4DF91029007284	FASTA	256	27,761
	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

References

	« Hide 'large scale' referencesShow '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] [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]	"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. , 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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[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] [Europe PMC] [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] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DEFFA. A93309.

RefSeq

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.

UniGene

Dm.6818.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MG5	X-ray	1.63	A/B	2-256	[»]

ProteinModelPortal

P00334.

SMR

P00334. Positions 2-256.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00334. 1 interaction.

MINT

MINT-877153.

Proteomic databases

PaxDb

P00334.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3771877.

KEGG

dme:Dmel_CG3481.

Organism-specific databases

CTD

3771877.

FlyBase

FBgn0000055. Adh.

Phylogenomic databases

eggNOG

COG1028.

InParanoid

P00334.

KO

K00001.

OrthoDB

EOG40K6FN.

Enzyme and pathway databases

SABIO-RK

P00334.

Gene expression databases

GermOnline

CG3481. Drosophila melanogaster.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002425. ADH_Drosophila-type.
IPR002424. ADH_insect.
IPR002198. DH_sc/Rdtase_SDR.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR01168. ALCDHDRGNASE.
PR01167. INSADHFAMILY.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00334.

GenomeRNAi

3771877.

NextBio

851589.

Entry information

Entry name

ADH_DROME

Accession

Primary (citable) accession number: P00334
Secondary accession number(s): A4V0Q1 , Q27332, Q27579, Q27596, Q2MGK2, Q53XD5, Q95TC8, Q9NKC0, Q9VJS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project