ADH_SCAAL
ID ADH_SCAAL Reviewed; 254 AA.
AC P25988;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh;
OS Scaptomyza albovittata (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Scaptomyza.
OX NCBI_TaxID=7299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1766364; DOI=10.1093/oxfordjournals.molbev.a040678;
RA Thomas R.H., Hunt J.A.;
RT "The molecular evolution of the alcohol dehydrogenase locus and the
RT phylogeny of Hawaiian Drosophila.";
RL Mol. Biol. Evol. 8:687-702(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8487635; DOI=10.1093/oxfordjournals.molbev.a040008;
RA Thomas R.H., Hunt J.A.;
RT "Phylogenetic relationships in Drosophila: a conflict between molecular and
RT morphological data.";
RL Mol. Biol. Evol. 10:362-374(1993).
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; M80925; AAA29953.1; -; Genomic_DNA.
DR PIR; A46276; A46276.
DR AlphaFoldDB; P25988; -.
DR SMR; P25988; -.
DR FlyBase; FBgn0013333; Salb\Adh.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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 CHAIN 1..254
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000054515"
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; 27462 MW; 30C4621CE697A793 CRC64;
MCIAGKNIIF VAGLGGIGLD TNREIVKSGP KNLVILDRIE NPAAIAELQA INPNVTVSFY
PYDVTVALAE SVKLLKTIFA KLKTVDLLVN GAGILDDHQI ERTIAVNFTG TVNTTTAIME
FWDKRKGGPG GVIANICSVT GFNSIYQVPV YSASKAAALS FTSSLARLAP ITGVTVYSIN
PGITDTTLVH KFNSWLDVEP RVAEKLLAFP TQTSLACAKN FVRAIEANKN GAIWKLDLNR
LDEIEWTKHW DSGI