ID ADH_DROFL Reviewed; 254 AA. AC P48585; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 93. DE RecName: Full=Alcohol dehydrogenase; DE EC=1.1.1.1; GN Name=Adh; OS Drosophila flavomontana (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila. OX NCBI_TaxID=40367; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8583887; DOI=10.1093/oxfordjournals.molbev.a025551; RA Nurminsky D.I., Moriyama E.N., Lozovskaya E.R., Hartl D.L.; RT "Molecular phylogeny and genome evolution in the Drosophila virilis species RT group: duplications of the alcohol dehydrogenase gene."; RL Mol. Biol. Evol. 13:132-149(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NAD(+) = an aldehyde + NADH + H(+); 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 + NADH + H(+); 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; U26838; AAB02624.1; -; Genomic_DNA. DR AlphaFoldDB; P48585; -. DR SMR; P48585; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA. DR CDD; cd05323; ADH_SDR_c_like; 1. DR FunFam; 3.40.50.720:FF:000302; Alcohol dehydrogenase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 PANTHER; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1. DR PANTHER; PTHR44229:SF8; ALCOHOL DEHYDROGENASE-RELATED; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR01168; ALCDHDRGNASE. DR PRINTS; PR01167; INSADHFAMILY. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..254 FT /note="Alcohol dehydrogenase" FT /id="PRO_0000054461" FT ACT_SITE 151 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 10..33 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 254 AA; 27578 MW; 3BFC223AC26F5A4F CRC64; MAIANKNIIF VAGLGGIGLD TSREIVKSGP KNLVILDRID NPTAIAELKA INPKVTVTFY PYDVTVPVAE TTKLLKTIFA QLKTVDLLIN GAGILDDHQI ERTIAVNFTG TVNTTTAIME FWDKRKGGPG GVIANICSVT GFNAIYQVPV YSASKAAALS FTNSLARLAP ITGVTAYSIN PGITRTPLVH RFNSWLDVEP RVGELLLEHP TQTTLECAQN FVKAIEANKN GAIWQLDLGQ LIAVEWTKHW DSHI //