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DROME:ADH

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) Adh
Protein Name(s) Alcohol dehydrogenase
External Links
UniProt P00334
EMBL M17827
M17828
M19547
M17830
M17831
M17832
M17833
M17834
M17835
M17836
M17837
Z00030
M22210
M57239
X78384
M36580
X60791
X60792
X60793
U20765
X98338
AF175211
AF175212
AF175213
AF175214
AF175215
AF175216
AF175217
AF175218
AF175219
AF175220
AE014134
AE014134
AE014134
AE014134
AY060227
BT012435
M17845
PIR A93309
RefSeq NP_001027266.1
NP_001027267.1
NP_001027268.1
NP_001027269.1
NP_001027270.1
UniGene Dm.6818
PDB 1MG5
PDBsum 1MG5
ProteinModelPortal P00334
SMR P00334
BioGrid 533474
IntAct P00334
MINT MINT-877153
PaxDb P00334
PRIDE P00334
GeneID 3771877
KEGG dme:Dmel_CG3481
CTD 3771877
FlyBase FBgn0000055
eggNOG COG1028
InParanoid P00334
KO K00001
OrthoDB EOG7966HT
PhylomeDB P00334
Reactome REACT_184367
REACT_207120
SABIO-RK P00334
EvolutionaryTrace P00334
GenomeRNAi 3771877
NextBio 851589
Proteomes UP000000803
GO GO:0005829
GO:0005811
GO:0005875
GO:0043234
GO:0004022
GO:0042803
GO:0046164
GO:0006066
GO:0048149
Gene3D 3.40.50.720
InterPro IPR002425
IPR002424
IPR002198
IPR016040
IPR020904
Pfam PF00106
PRINTS PR01168
PR01167
PR00080
PROSITE PS00061

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0046164

alcohol catabolic process

PMID:8461298[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:8461298[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002451405
SGD:S000004839

F

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:10471707[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:8353517[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006067

ethanol metabolic process

DOI:10.1016/0965-1748(92)90115-U

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

DOI:10.1016/0965-1748(92)90115-U

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008774

acetaldehyde dehydrogenase (acetylating) activity

DOI:10.1016/0965-1748(92)90115-U

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006117

acetaldehyde metabolic process

DOI:10.1016/0965-1748(92)90115-U

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006069

ethanol oxidation

DOI:10.1007/BF00127499

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008774

acetaldehyde dehydrogenase (acetylating) activity

DOI:10.1007/BF00127499

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

DOI:10.1007/BF00127499

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006117

acetaldehyde metabolic process

DOI:10.1007/BF00127499

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:6807351[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006066

alcohol metabolic process

PMID:6807351[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:15581900[6]

ECO:0000353

physical interaction evidence used in manual assertion

FB:FBgn0000055

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:15581900[6]

ECO:0000353

physical interaction evidence used in manual assertion

FB:FBgn0000055

C

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:12972637[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0048149

behavioral response to ethanol

PMID:12486199[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:109448[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

PMID:109448[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:109448[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002424
InterPro:IPR002425

F

Seeded From UniProt

complete

involved_in

GO:0006066

alcohol metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002425

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020904

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002424
InterPro:IPR002425

P

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.1

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Chen, Z et al. (1993) Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32 3342-6 PubMed GONUTS page
  2. ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ Ashburner, M et al. (1999) An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region. Genetics 153 179-219 PubMed GONUTS page
  4. ↑ Leal, JF & Barbancho, M (1993) Aldehyde dehydrogenase (ALDH) activity in Drosophila melanogaster adults: evidence for cytosolic localization. Insect Biochem. Mol. Biol. 23 543-7 PubMed GONUTS page
  5. ↑ 5.0 5.1 Winberg, JO et al. (1982) Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF. Biochim. Biophys. Acta 704 7-16 PubMed GONUTS page
  6. ↑ 6.0 6.1 Benach, J et al. (2005) Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis. J. Mol. Biol. 345 579-98 PubMed GONUTS page
  7. ↑ Chen, Y & Stephan, W (2003) Compensatory evolution of a precursor messenger RNA secondary structure in the Drosophila melanogaster Adh gene. Proc. Natl. Acad. Sci. U.S.A. 100 11499-504 PubMed GONUTS page
  8. ↑ Wolf, FW et al. (2002) High-resolution analysis of ethanol-induced locomotor stimulation in Drosophila. J. Neurosci. 22 11035-44 PubMed GONUTS page
  9. ↑ 9.0 9.1 9.2 Lee, CY et al. (1979) Biochemical analyses of natural and induced null variants of Drosophila enzymes. J. Biol. Chem. 254 6375-81 PubMed GONUTS page
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