ADH1_DROMT
ID ADH1_DROMT Reviewed; 254 AA.
AC P22246;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
GN Name=Adh1;
OS Drosophila mettleri (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7228;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1775067; DOI=10.1093/oxfordjournals.molbev.a040692;
RA Yum J., Starmer W.T., Sullivan D.T.;
RT "The structure of the Adh locus of Drosophila mettleri: an intermediate in
RT the evolution of the Adh locus in the repleta group of Drosophila.";
RL Mol. Biol. Evol. 8:857-867(1991).
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; M57300; AAA28364.1; -; Genomic_DNA.
DR PIR; A40553; A40553.
DR AlphaFoldDB; P22246; -.
DR SMR; P22246; -.
DR FlyBase; FBgn0012533; Dmet\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_0000054480"
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; 27539 MW; BB0D26CB95649D86 CRC64;
MAIANKNIIF VAGLGGIGLD TSREIVKSGP KNLVILDRVE NPTAIAELKA INPKVTITFY
PYDVTVSVAE STKLLKTIFD KLKTVDLLIN GAGILDDYQI ERTIAVNFAG TVNTTTAIMA
FWDKRKGGPG GVIANICSVT GFNSIYQVPV YSASKAAAIS FTNSLAKLAP ITGVTAYSIN
PGITKTPLVH KFNSWLDVEP RVAELLLEHP TQTTLQCAQN FVKAIEANKN GAIWKLDLGR
LDAIEWTQHW DSHI