ADH_DROWI
ID ADH_DROWI Reviewed; 254 AA.
AC Q05114; B4MZ46; Q9NG34; Q9TVL4; Q9TW33; Q9TY28; Q9TY29; Q9TY30; Q9TY31;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh; ORFNames=GK18290;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W4L;
RX PubMed=8336545; DOI=10.1093/oxfordjournals.molbev.a040027;
RA Anderson C.L., Carew E., Powell J.R.;
RT "Evolution of the Adh locus in the Drosophila willistoni group: the loss of
RT an intron, and shift in codon usage.";
RL Mol. Biol. Evol. 10:605-618(1993).
RN [2]
RP SEQUENCE REVISION.
RA Powell J.R.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-57; ALA-77; PRO-138;
RP PRO-194; ALA-213 AND THR-225.
RC STRAIN=0811.0, 0811.4, A57, Atlixco, Belize II, Belize VI, Cano Mora,
RC Guana, Lima, Manaus I, Manaus II, Manaus III, Manaus IV, PA1, PA2, PA3, and
RC W3L;
RX PubMed=9302316; DOI=10.1007/pl00006225;
RA Griffith E.C., Powell J.R.;
RT "Adh nucleotide variation in Drosophila willistoni: high replacement
RT polymorphism in an electrophoretically monomorphic protein.";
RL J. Mol. Evol. 45:232-237(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-57; ALA-77; PRO-138;
RP PRO-194; ALA-213 AND THR-225.
RC STRAIN=0811.0, 0811.4, A57, Atlixco, Belize II, Belize VI, Cano Mora,
RC Guana, Lima, Manaus I, Manaus II, Manaus III, Manaus IV, PA1, PA2, PA3, and
RC W3L;
RX AGRICOLA=IND21806050; DOI=10.2307/2411239;
RA Gleason J.M., Griffith E.C., Powell J.R.;
RT "A molecular phylogeny of the Drosophila willistoni group: conflicts
RT between species concepts?";
RL Evolution 52:1093-1103(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-166.
RA O'Grady P.M.;
RT "Phylogenetic relationships of flies in family Drosophilidae inferred by
RT combined analysis of morphological and molecular characters.";
RL Thesis (2000), University of Arizona / Tucson, United States.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L08648; AAA91100.1; -; Genomic_DNA.
DR EMBL; U95251; AAD00777.1; -; Genomic_DNA.
DR EMBL; U95252; AAD00778.1; -; Genomic_DNA.
DR EMBL; U95253; AAD00779.1; -; Genomic_DNA.
DR EMBL; U95254; AAD00780.1; -; Genomic_DNA.
DR EMBL; U95255; AAD00781.1; -; Genomic_DNA.
DR EMBL; U95256; AAD00782.1; -; Genomic_DNA.
DR EMBL; U95257; AAD00783.1; -; Genomic_DNA.
DR EMBL; U95258; AAD00784.1; -; Genomic_DNA.
DR EMBL; U95259; AAD00785.1; -; Genomic_DNA.
DR EMBL; U95260; AAD00786.1; -; Genomic_DNA.
DR EMBL; U95261; AAD00787.1; -; Genomic_DNA.
DR EMBL; U95262; AAD00788.1; -; Genomic_DNA.
DR EMBL; U95263; AAD00789.1; -; Genomic_DNA.
DR EMBL; U95264; AAD00790.1; -; Genomic_DNA.
DR EMBL; U95265; AAD00791.1; -; Genomic_DNA.
DR EMBL; U95266; AAD00792.1; -; Genomic_DNA.
DR EMBL; U95267; AAD00793.1; -; Genomic_DNA.
DR EMBL; CH963913; EDW77442.1; -; Genomic_DNA.
DR EMBL; AF264082; AAF72724.1; -; Genomic_DNA.
DR RefSeq; XP_002066456.1; XM_002066420.2.
DR RefSeq; XP_015033661.1; XM_015178175.1.
DR AlphaFoldDB; Q05114; -.
DR SMR; Q05114; -.
DR STRING; 7260.FBpp0247433; -.
DR EnsemblMetazoa; FBtr0248941; FBpp0247433; FBgn0013152.
DR EnsemblMetazoa; FBtr0417483; FBpp0375647; FBgn0013152.
DR GeneID; 6643501; -.
DR KEGG; dwi:6643501; -.
DR eggNOG; KOG4169; Eukaryota.
DR HOGENOM; CLU_010194_2_16_1; -.
DR InParanoid; Q05114; -.
DR OMA; TTLQCAQ; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; Q05114; -.
DR ChiTaRS; Adh; fly.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblMetazoa.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:EnsemblMetazoa.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0006117; P:acetaldehyde metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0046164; P:alcohol catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:EnsemblMetazoa.
DR GO; GO:0006069; P:ethanol oxidation; IEA:EnsemblMetazoa.
DR GO; GO:0006734; P:NADH metabolic process; IEA:EnsemblMetazoa.
DR InterPro; IPR002425; ADH_Drosophila-type.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR01168; ALCDHDRGNASE.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..254
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000054500"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 9..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 57
FT /note="V -> I (in strain: 0811.4)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT VARIANT 77
FT /note="T -> A (in strain: 0811.0 and Lima)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT VARIANT 138
FT /note="S -> P (in strain: Manaus I)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT VARIANT 194
FT /note="S -> P (in strain: Manaus III)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT VARIANT 213
FT /note="T -> A (in strain: Cano Mora and Atlixco)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT VARIANT 225
FT /note="I -> T (in strain: A57)"
FT /evidence="ECO:0000269|PubMed:9302316, ECO:0000269|Ref.4"
FT CONFLICT 41
FT /note="N -> K (in Ref. 6; AAF72724)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="K -> N (in Ref. 6; AAF72724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27620 MW; C20FDF95E89D6E16 CRC64;
MALTNKNIIF VAGLGGIGLD TSRELVKRDL KNLVILDRID NPAAIAELKA INPKVTVTFY
PYDVTTPLTE TTKLLKTIFA QLKTVDVLIN GAGILDDHQI ERTIAVNFTG LVNTTTAILD
FWDKRKGGPG GVICNIGSVT GFNAIYQVPV YSASKAAVVS FTQSIAKLAN VTGVTAFTVN
PGITKTTLVH KFNSWLDVET RVAEKLLEHP TQTTLACAQN FVKAIELNKN GAIWKLDLGT
LEPIEWTKHW DSGI
