ID   ADH_DROPU               Reviewed;         254 AA.
AC   Q9U8S9; Q9NG38;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Alcohol dehydrogenase;
DE            EC=1.1.1.1;
GN   Name=Adh;
OS   Drosophila paulistorum (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46793 {ECO:0000312|EMBL:AAD00796.1};
RN   [1] {ECO:0000312|EMBL:AAD00796.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=0771.4 {ECO:0000312|EMBL:AAD00796.1},
RC   Andean-Brazilian {ECO:0000312|EMBL:AAD00797.1}, and
RC   Tame {ECO:0000312|EMBL:AAD00798.1};
RX   AGRICOLA=IND21806050; DOI=10.2307/2411239;
RA   Gleason J.M., Griffith E.C., Powell J.R.;
RT   "A molecular phylogeny of the Drosophila willistoni group: conflicts
RT   between species concepts?";
RL   Evolution 52:1093-1103(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-248.
RX   PubMed=10948268; DOI=10.1007/s002390010072;
RA   Katoh T., Tamura K., Aotsuka T.;
RT   "Phylogenetic position of the subgenus Lordiphosa of the genus Drosophila
RT   (Diptera: Drosophilidae) inferred from alcohol dehydrogenase (Adh) gene
RT   sequences.";
RL   J. Mol. Evol. 51:122-130(2000).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-166.
RA   O'Grady P.M.;
RT   "Phylogenetic relationships of flies in family Drosophilidae inferred by
RT   combined analysis of morphological and molecular characters.";
RL   Thesis (2000), University of Arizona / Tucson, United States.
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, ECO:0000305};
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, ECO:0000305};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000255|RuleBase:RU000363, ECO:0000305}.
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DR   EMBL; U95270; AAD00796.1; -; Genomic_DNA.
DR   EMBL; U95271; AAD00797.1; -; Genomic_DNA.
DR   EMBL; U95272; AAD00798.1; -; Genomic_DNA.
DR   EMBL; AB026529; BAA85831.1; -; Genomic_DNA.
DR   EMBL; AF264078; AAF72720.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U8S9; -.
DR   SMR; Q9U8S9; -.
DR   FlyBase; FBgn0016290; Dpau\Adh.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0046164; P:alcohol catabolic process; ISS:UniProtKB.
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   CHAIN           1..254
FT                   /note="Alcohol dehydrogenase"
FT                   /id="PRO_0000054492"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q05114"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        41
FT                   /note="N -> K (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="I -> M (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="T -> I (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="N -> K (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="V -> I (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="I -> M (in Ref. 3; AAF72720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="E -> G (in Ref. 2; BAA85831)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  27620 MW;  C20FDF95E89D6E16 CRC64;
     MALTNKNIIF VAGLGGIGLD TSRELVKRDL KNLVILDRID NPAAIAELKA INPKVTVTFY
     PYDVTTPLTE TTKLLKTIFA QLKTVDVLIN GAGILDDHQI ERTIAVNFTG LVNTTTAILD
     FWDKRKGGPG GVICNIGSVT GFNAIYQVPV YSASKAAVVS FTQSIAKLAN VTGVTAFTVN
     PGITKTTLVH KFNSWLDVET RVAEKLLEHP TQTTLACAQN FVKAIELNKN GAIWKLDLGT
     LEPIEWTKHW DSGI