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ADH_DROEQ
ID   ADH_DROEQ               Reviewed;         254 AA.
AC   Q9NG42;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Alcohol dehydrogenase;
DE            EC=1.1.1.1;
GN   Name=Adh;
OS   Drosophila equinoxialis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46790 {ECO:0000312|EMBL:AAD00794.1};
RN   [1] {ECO:0000312|EMBL:AAD00794.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=0741.0 {ECO:0000312|EMBL:AAD00794.1}, and
RC   Puerto Rico {ECO:0000312|EMBL:AAD00795.1};
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 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; U95268; AAD00794.1; -; Genomic_DNA.
DR   EMBL; U95269; AAD00795.1; -; Genomic_DNA.
DR   EMBL; AF264074; AAF72716.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NG42; -.
DR   SMR; Q9NG42; -.
DR   FlyBase; FBgn0016178; Dequ\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_0000054459"
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        157
FT                   /note="A -> R (in Ref. 2; AAF72716)"
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
 
 
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