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P00334

- ADH_DROME

UniProt

P00334 - ADH_DROME

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Protein

Alcohol dehydrogenase

Gene

Adh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi133 – 1331G → I: Complete loss of activity. 1 Publication
Mutagenesisi136 – 1361C → A: No decrease in activity. 1 Publication
Mutagenesisi153 – 1531Y → C: Retains only 0.25% activity. 3 Publications
Mutagenesisi153 – 1531Y → F, H, E or Q: Complete loss of activity. 3 Publications
Mutagenesisi157 – 1571K → I: Complete loss of activity. 2 Publications
Mutagenesisi157 – 1571K → R: Retains only 2.2% activity. 2 Publications
Mutagenesisi184 – 1841G → L: Complete loss of activity. 1 Publication
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 – 135Combined sources
Turni14 – 163Combined sources
Helixi18 – 2710Combined sources
Beta strandi33 – 408Combined sources
Helixi44 – 5310Combined sources
Beta strandi57 – 637Combined sources
Helixi70 – 8415Combined sources
Beta strandi89 – 924Combined sources
Helixi102 – 1098Combined sources
Helixi111 – 12414Combined sources
Helixi126 – 1283Combined sources
Beta strandi133 – 1386Combined sources
Helixi141 – 1433Combined sources
Helixi151 – 17424Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi185 – 1884Combined sources
Turni189 – 1924Combined sources
Helixi197 – 1993Combined sources
Helixi204 – 2096Combined sources
Helixi216 – 22914Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi242 – 2454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL
60 70 80 90 100
KAINPKVTVT FYPYDVTVPI AETTKLLKTI FAQLKTVDVL INGAGILDDH
110 120 130 140 150
QIERTIAVNY TGLVNTTTAI LDFWDKRKGG PGGIICNIGS VTGFNAIYQV
160 170 180 190 200
PVYSGTKAAV VNFTSSLAKL APITGVTAYT VNPGITRTTL VHKFNSWLDV
210 220 230 240 250
EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL GTLEAIQWTK

HWDSGI
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:
EMBLi
GenBanki
DDBJi
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_001032095.2.
NP_001027267.1. NM_001032096.2.
NP_001027268.1. NM_001032097.2.
NP_001027269.1. NM_001032098.2.
NP_001027270.1. NM_001032099.2.
UniGeneiDm.6818.

Genome annotation databases

GeneIDi3771877.
KEGGidme:Dmel_CG3481.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001032095.2.
NP_001027267.1. NM_001032096.2.
NP_001027268.1. NM_001032097.2.
NP_001027269.1. NM_001032098.2.
NP_001027270.1. NM_001032099.2.
UniGenei Dm.6818.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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