ID   ADH2_DROBU              Reviewed;         254 AA.
AC   P25720;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
GN   Name=Adh2;
OS   Drosophila buzzatii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dorit R.L., Ayala F.J. III, Gilbert W.;
RT   "ADH-2 sequence evolution in the Drosophila mulleri subgroup.";
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
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; M62743; AAA28328.1; -; Genomic_DNA.
DR   AlphaFoldDB; P25720; -.
DR   SMR; P25720; -.
DR   FlyBase; FBgn0012231; Dbuz\Adh2.
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                   /evidence="ECO:0000250"
FT   CHAIN           2..254
FT                   /note="Alcohol dehydrogenase 2"
FT                   /id="PRO_0000054456"
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;  27519 MW;  51A138BCD0F2EC93 CRC64;
     MAIANKNIIF VAGLGGIGFD TSREIVKSGP KNLVILDRIE NPAAIAELKA LNPKVTVTFY
     PYDVTVPVAE TTKLLKTIFD KLKTVDLLIN GAGILDDYQI ERTIAVNFTG TVNTTTAIMA
     FWDKRKGGPG GVIANICSVT GFNAIYQVPV YSASKAAALS FTNSLAKLAP ITGVTAYSIN
     PGITKTTLVH KFNSWLDVEP RVAELLLEHP TQTTLQCAQN FVKAIEANQN GAIWKLDLGR
     LEAIEWTKHW DSGI