ADH_DROIN
ID ADH_DROIN Reviewed; 254 AA.
AC Q9NG40;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh;
OS Drosophila insularis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46792 {ECO:0000312|EMBL:AAD00799.1};
RN [1] {ECO:0000312|EMBL:AAD00799.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FA {ECO:0000312|EMBL:AAD00799.1};
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; U95273; AAD00799.1; -; Genomic_DNA.
DR EMBL; AF264076; AAF72718.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9NG40; -.
DR SMR; Q9NG40; -.
DR FlyBase; FBgn0016214; Dins\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_0000054469"
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 35
FT /note="I -> V (in Ref. 2; AAF72718)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="AA -> ED (in Ref. 2; AAF72718)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> C (in Ref. 2; AAF72718)"
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
