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UniProtKB/Swiss-Prot entry P10807

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADH_DROLE
Primary accession number P10807
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 70)
Name and origin of the protein
Protein name Alcohol dehydrogenase
Synonym EC 1.1.1.1
Gene name
Name: Adh
From
Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis) [TaxID: 7225] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Scaptodrosophila.
Protein existence 1: Evidence at protein level;
References
[1]
 PROTEIN SEQUENCE.
DOI=10.1111/j.1432-1033.1989.tb14632.x; PubMed=2707261 [NCBI, ExPASy, EBI, Israel, Japan]
Villarroya A., Juan E., Egestad B., Joernvall H.;
"The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.";
Eur. J. Biochem. 180:191-197(1989).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=323G;
DOI=10.1093/nar/18.21.6420; PubMed=2243785 [NCBI, ExPASy, EBI, Israel, Japan]
Juan E., Papaceit M., Quintana A.;
"Nucleotide sequence of the Adh gene of Drosophila lebanonensis.";
Nucleic Acids Res. 18:6420-6420(1990).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/18.22.6706; PubMed=2251140 [NCBI, ExPASy, EBI, Israel, Japan]
Albalat R., Gonzalez-Duarte R.;
"Nucleotide sequence of the Adh gene of Drosophila lebanonensis.";
Nucleic Acids Res. 18:6706-6706(1990).
[4]
 ERRATUM.
DOI=10.1093/nar/19.2.424; PubMed=1849634 [NCBI, ExPASy, EBI, Israel, Japan]
Albalat R., Gonzalez-Duarte R.;
Nucleic Acids Res. 19:424-424(1991).
[5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(93)90364-9; PubMed=8482531 [NCBI, ExPASy, EBI, Israel, Japan]
Albalat R., Gonzalez-Duarte R.;
"Adh and Adh-dup sequences of Drosophila lebanonensis and D. immigrans: interspecies comparisons.";
Gene 126:171-178(1993).
[6]
 PHYLOGENETIC RELATIONSHIP TO OTHER DROSOPHILA ADH.
DOI=10.1007/BF02101282; PubMed=1904097 [NCBI, ExPASy, EBI, Israel, Japan]
Villarroya A., Juan E.;
"ADH and phylogenetic relationships of Drosophila lebanonesis (Scaptodrosophila).";
J. Mol. Evol. 32:421-428(1991).
[7]
 X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
DOI=10.1006/jmbi.1998.2015; PubMed=9735295 [NCBI, ExPASy, EBI, Israel, Japan]
Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.;
"The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9-A resolution.";
J. Mol. Biol. 282:383-399(1998).
[8]
 X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH NAD AND PRODUCT.
DOI=10.1006/jmbi.1999.2765; PubMed=10366509 [NCBI, ExPASy, EBI, Israel, Japan]
Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.;
"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.";
J. Mol. Biol. 289:335-355(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X53429; CAA37520.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54814; CAA38583.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M97637; AAA28355.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S12695; DEFFRL.
3D structure databases
PDB
1A4U; X-ray; 1.92 A; A/B=1-254.[ExPASy / RCSB / EBI]
1B14; X-ray; 2.40 A; A/B=1-254.[ExPASy / RCSB / EBI]
1B15; X-ray; 2.20 A; A/B=1-254.[ExPASy / RCSB / EBI]
1B16; X-ray; 1.40 A; A/B=1-254.[ExPASy / RCSB / EBI]
1B2L; X-ray; 1.60 A; A=1-254.[ExPASy / RCSB / EBI]
1SBY; X-ray; 1.10 A; A/B=1-254.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A4U; -.
1B14; -.
1B15; -.
1B16; -.
1B2L; -.
1SBY; -.
ModBase P10807.
Organism-specific databases
FlyBase FBgn0012438; Dleb\Adh.
Ontologies
GO
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006066; Biological process: cellular alcohol metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002425; Insect_AlcDHase.
IPR002424; Insect_AlcDHase_fam.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR01168; ALCDHDRGNASE.
PR01167; INSADHFAMILY.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
Other
LinkHub P10807; -.
ProtoNet P10807.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   254  254     Alcohol dehydrogenase. PRO_0000054471
NP_BIND   10    33  24     NAD. 
ACT_SITE   151   151        Proton acceptor. 
BINDING   138   138        Substrate. 
MOD_RES   1     1        N-acetylmethionine. 
STRAND   7    11  5      
TURN   12    14  3      
HELIX   16    27  12      
STRAND   31    39  9      
HELIX   42    51  10      
STRAND   55    61  7      
HELIX   68    82  15      
STRAND   87    90  4      
HELIX   100   107  8      
HELIX   109   122  14      
HELIX   124   126  3      
STRAND   131   136  6      
HELIX   139   141  3      
HELIX   149   172  24      
STRAND   173   181  9      
STRAND   183   186  4      
STRAND   189   191  3      
HELIX   195   197  3      
HELIX   202   206  5      
HELIX   214   227  14      
STRAND   233   237  5      
STRAND   240   243  4      
Sequence information
Length: 254 AA [This is the length of the unprocessed precursor] Molecular weight: 27792 Da [This is the MW of the unprocessed precursor] CRC64: 56DA3644E6B9CDCE [This is a checksum on the sequence] 
        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
P10807 in FASTA format

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