ID   ADH2_DROMU              Reviewed;         254 AA.
AC   P07160;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   22-FEB-2023, entry version 103.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
GN   Name=Adh2;
OS   Drosophila mulleri (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2997730; DOI=10.1093/nar/13.19.6899;
RA   Fischer J.A., Maniatis T.;
RT   "Structure and transcription of the Drosophila mulleri alcohol
RT   dehydrogenase genes.";
RL   Nucleic Acids Res. 13:6899-6917(1985).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X03048; CAA26856.1; -; Genomic_DNA.
DR   PIR; A24268; A24268.
DR   AlphaFoldDB; P07160; -.
DR   SMR; P07160; -.
DR   FlyBase; FBgn0012582; Dmul\Adh2.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR   CDD; cd05323; ADH_SDR_c_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PANTHER; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   PANTHER; PTHR44229:SF8; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR01168; ALCDHDRGNASE.
DR   PRINTS; PR01167; INSADHFAMILY.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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..254
FT                   /note="Alcohol dehydrogenase 2"
FT                   /id="PRO_0000054482"
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;  27592 MW;  F5A9A7FD0FA23766 CRC64;
     MVIANKNIIF VAGLGGIGFD TSREIVKSGP KNLVILDRIE NPAAIAELKA LNPKVTVTFY
     PYDVTVSVAE TTKLLKTIFD KLKTVDLLIN GAGILDDYQI ERTIAVNFTG TVNTTTAIMS
     FWDKRKGGPG GIIANICSVT GFNAIYQVPV YSASKAAALS FTNSLAKLAP ITGVTAYSIN
     PGITKTTLVH KFNSWLDVEP RVAELLLEHP TQTTLQCAQN FVKAIEANQN GAIWKLDLGT
     LEAIEWTKHW DSHI
//