ID   ADH_DROMA               Reviewed;         256 AA.
AC   P07162; Q24233;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alcohol dehydrogenase;
DE            EC=1.1.1.1;
GN   Name=Adh;
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
RN   [1]
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   [2]
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   [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=1664000; DOI=10.1007/bf02102804;
RA   Maruyama K., Hartl D.L.;
RT   "Evidence for interspecific transfer of the transposable element mariner
RT   between Drosophila and Zaprionus.";
RL   J. Mol. Evol. 33:514-524(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; Z00033; CAA77334.1; -; Genomic_DNA.
DR   EMBL; M19264; AAA28332.1; -; Genomic_DNA.
DR   EMBL; X63953; CAA45374.1; -; Genomic_DNA.
DR   PIR; S09633; S09633.
DR   AlphaFoldDB; P07162; -.
DR   SMR; P07162; -.
DR   FlyBase; FBgn0012496; Dmau\Adh.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
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   CHAIN           2..256
FT                   /note="Alcohol dehydrogenase"
FT                   /id="PRO_0000054472"
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        246
FT                   /note="I -> V (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  27761 MW;  31DE52FB08656863 CRC64;
     MAFTLTNKNV IFVAGLGGIG LDTSKELVKR DLKNLVILDR IENPAAIAEL QAINPKVTVT
     FYPYDVTVPI AETTKLLKTI FAKLKTVDVL INGAGILDDH QIERTIAVNY TGLVNTTTAI
     LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT
     VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL
     STLEAIQWTK HWDSGI