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Reviewed, UniProtKB/Swiss-Prot P10807 (ADH_DROLE)

Last modified September 22, 2009. Version 73. 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
OrganismDrosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis)
Taxonomic identifier7225 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeScaptodrosophila

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Alcohol dehydrogenase
PRO_0000054471

Regions

Nucleotide binding10 – 3324NAD

Sites

Active site1511Proton acceptor
Binding site1381Substrate

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Secondary structure

........................................... 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10807-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 56DA3644E6B9CDCE

FASTA25427,792
        10         20         30         40         50         60 
MDLTNKNVIF VAALGGIGLD TSRELVKRNL KNFVILDRVE NPTALAELKA INPKVNITFH 

        70         80         90        100        110        120 
TYDVTVPVAE SKKLLKKIFD QLKTVDILIN GAGILDDHQI ERTIAINFTG LVNTTTAILD 

       130        140        150        160        170        180 
FWDKRKGGPG GIIANICSVT GFNAIHQVPV YSASKAAVVS FTNSLAKLAP ITGVTAYSIN 

       190        200        210        220        230        240 
PGITRTPLVH TFNSWLDVEP RVAELLLSHP TQTSEQCGQN FVKAIEANKN GAIWKLDLGT 

       250 
LEAIEWTKHW DSHI 

« Hide

References

[1]"The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc."
Villarroya A., Juan E., Egestad B., Joernvall H.
Eur. J. Biochem. 180:191-197(1989) [PubMed: 2707261] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Nucleotide sequence of the Adh gene of Drosophila lebanonensis."
Juan E., Papaceit M., Quintana A.
Nucleic Acids Res. 18:6420-6420(1990) [PubMed: 2243785] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 323G.
[3]"Nucleotide sequence of the Adh gene of Drosophila lebanonensis."
Albalat R., Gonzalez-Duarte R.
Nucleic Acids Res. 18:6706-6706(1990) [PubMed: 2251140] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Erratum
Albalat R., Gonzalez-Duarte R.
Nucleic Acids Res. 19:424-424(1991) [PubMed: 1849634] [Abstract]
[5]"Adh and Adh-dup sequences of Drosophila lebanonensis and D. immigrans: interspecies comparisons."
Albalat R., Gonzalez-Duarte R.
Gene 126:171-178(1993) [PubMed: 8482531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"ADH and phylogenetic relationships of Drosophila lebanonesis (Scaptodrosophila)."
Villarroya A., Juan E.
J. Mol. Evol. 32:421-428(1991) [PubMed: 1904097] [Abstract]
Cited for: PHYLOGENETIC RELATIONSHIP TO OTHER DROSOPHILA ADH.
[7]"The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9-A resolution."
Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.
J. Mol. Biol. 282:383-399(1998) [PubMed: 9735295] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
[8]"The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4-A resolution by X-ray crystallography."
Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.
J. Mol. Biol. 289:335-355(1999) [PubMed: 10366509] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH NAD AND PRODUCT.

Cross-references

Sequence databases

X53429 Genomic DNA. Translation: CAA37520.1. Sequence problems.
X54814 Genomic DNA. Translation: CAA38583.1.
M97637 Genomic DNA. Translation: AAA28355.1.
PIRDEFFRL. S12695.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A4UX-ray1.92A/B1-254[»]
1B14X-ray2.40A/B1-254[»]
1B15X-ray2.20A/B1-254[»]
1B16X-ray1.40A/B1-254[»]
1B2LX-ray1.60A1-254[»]
1SBYX-ray1.10A/B1-254[»]
ModBaseSearch...

Organism-specific databases

FlyBaseFBgn0012438. Dleb\Adh.

Enzyme and pathway databases

BRENDA1.1.1.1. 189313.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002425. Insect_ADH.
IPR002424. Insect_AlcDH_fam.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR01168. ALCDHDRGNASE.
PR01167. INSADHFAMILY.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH_DROLE
AccessionPrimary (citable) accession number: P10807
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 22, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents