ADH1_DROMN
ID ADH1_DROMN Reviewed; 254 AA.
AC P48586;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
GN Name=Adh1;
OS Drosophila montana (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=40370;
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 + 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; U26842; AAB02628.1; -; Genomic_DNA.
DR AlphaFoldDB; P48586; -.
DR SMR; P48586; -.
DR FlyBase; FBgn0013852; Dmon\Adh1.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..254
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000054476"
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; 27548 MW; 802059EFF27253CF CRC64;
MAIANKNIIF VAGLGGIGLD TSREIVKSGP KNLVILDRID NPTAIAELKA INPKVTVTFY
PYDVTVPVAE TIKLLKTIFA QLKTVDLLIN GAGILDDHQI ERTIAVNFTG TVNTTTAIME
FWDKRKGGPG GVVANICSVT GFNAIYQVPV YSASKAAALS FTNSLARLAP ITGVTAYSIN
PGITRTPLVH KFNSWLDVEP RVGELLLEHP TQTTLECAQN FVKAIEANKN GAIWQLDLGQ
LIAVEWTKHW DSHI