ADH_DROSI
ID ADH_DROSI Reviewed; 256 AA.
AC Q24641; B4Q5K9; P07163; Q6SE55;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh; ORFNames=GD23968;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6429340; DOI=10.1007/bf02101983;
RA Cohn V.H., Thompson M.A., Moore G.P.;
RT "Nucleotide sequence comparison of the Adh gene in three drosophilids.";
RL J. Mol. Evol. 20:31-37(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6427630; DOI=10.1038/309425a0;
RA Bodmer M., Ashburner M.;
RT "Conservation and change in the DNA sequences coding for alcohol
RT dehydrogenase in sibling species of Drosophila.";
RL Nature 309:425-430(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3367783; DOI=10.1093/oxfordjournals.molbev.a040487;
RA Cohn V.H., Moore G.P.;
RT "Organization and evolution of the alcohol dehydrogenase gene in
RT Drosophila.";
RL Mol. Biol. Evol. 5:154-166(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2124699; DOI=10.1073/pnas.87.24.9674;
RA Laurie C.C., Heath E.M., Jacobson J.W., Thomson M.S.;
RT "Genetic basis of the difference in alcohol dehydrogenase expression
RT between Drosophila melanogaster and Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9674-9678(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Australia, Brazzaville, France, and Ottawa;
RX PubMed=1904993; DOI=10.1038/351652a0;
RA McDonald J.H., Kreitman M.;
RT "Adaptive protein evolution at the Adh locus in Drosophila.";
RL Nature 351:652-654(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=14762063; DOI=10.1101/gr.1329204;
RA Halligan D.L., Eyre-Walker A., Andolfatto P., Keightley P.D.;
RT "Patterns of evolutionary constraints in intronic and intergenic DNA of
RT Drosophila.";
RL Genome Res. 14:273-279(2004).
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}.
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DR EMBL; X00607; CAA25249.1; -; Genomic_DNA.
DR EMBL; M19276; AAA28360.1; -; Genomic_DNA.
DR EMBL; M19263; AAA28337.1; -; Genomic_DNA.
DR EMBL; M36581; AAA28333.1; -; Genomic_DNA.
DR EMBL; X57361; CAA40635.1; -; Genomic_DNA.
DR EMBL; X57362; CAA40636.1; -; Genomic_DNA.
DR EMBL; X57363; CAA40637.1; -; Genomic_DNA.
DR EMBL; X57364; CAA40638.1; -; Genomic_DNA.
DR EMBL; CM000361; EDX05053.1; -; Genomic_DNA.
DR EMBL; AY459545; AAR23003.1; -; Genomic_DNA.
DR PIR; S18273; S18273.
DR RefSeq; XP_016024999.1; XM_016180148.1.
DR AlphaFoldDB; Q24641; -.
DR SMR; Q24641; -.
DR STRING; 7240.Q24641; -.
DR EnsemblMetazoa; FBtr0223878; FBpp0222370; FBgn0012824.
DR GeneID; 6732347; -.
DR HOGENOM; CLU_010194_2_16_1; -.
DR OMA; TTLQCAQ; -.
DR PhylomeDB; Q24641; -.
DR ChiTaRS; Adh; fly.
DR Proteomes; UP000000304; Chromosome 2l.
DR Bgee; FBgn0012824; Expressed in adult organism and 3 other tissues.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT CHAIN 2..256
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000054494"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 12..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="A -> V (in Ref. 2; AAA28360)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> N (in Ref. 2; AAA28360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 27745 MW; 2BEC8BDBFFD7E00B CRC64;
MAFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL KAINPKVTVT
FYPYDVTVPI AETTKLLKTI FAKLKTVDVL INGAGILDDH QIERTIAVNY TGLVNTTTAI
LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT
VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL
GTLEAIQWTK HWDSGI
