ADH_DROLE
ID ADH_DROLE Reviewed; 254 AA.
AC P10807;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh;
OS Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Scaptodrosophila.
OX NCBI_TaxID=7225;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=2707261; DOI=10.1111/j.1432-1033.1989.tb14632.x;
RA Villarroya A., Juan E., Egestad B., Joernvall H.;
RT "The primary structure of alcohol dehydrogenase from Drosophila
RT lebanonensis. Extensive variation within insect 'short-chain' alcohol
RT dehydrogenase lacking zinc.";
RL Eur. J. Biochem. 180:191-197(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=323G;
RX PubMed=2243785; DOI=10.1093/nar/18.21.6420;
RA Juan E., Papaceit M., Quintana A.;
RT "Nucleotide sequence of the Adh gene of Drosophila lebanonensis.";
RL Nucleic Acids Res. 18:6420-6420(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2251140; DOI=10.1093/nar/18.22.6706;
RA Albalat R., Gonzalez-Duarte R.;
RT "Nucleotide sequence of the Adh gene of Drosophila lebanonensis.";
RL Nucleic Acids Res. 18:6706-6706(1990).
RN [4]
RP ERRATUM OF PUBMED:2251140.
RX PubMed=1849634; DOI=10.1093/nar/19.2.424;
RA Albalat R., Gonzalez-Duarte R.;
RL Nucleic Acids Res. 19:424-424(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8482531; DOI=10.1016/0378-1119(93)90364-9;
RA Albalat R., Gonzalez-Duarte R.;
RT "Adh and Adh-dup sequences of Drosophila lebanonensis and D. immigrans:
RT interspecies comparisons.";
RL Gene 126:171-178(1993).
RN [6]
RP PHYLOGENETIC RELATIONSHIP TO OTHER DROSOPHILA ADH.
RX PubMed=1904097; DOI=10.1007/bf02101282;
RA Villarroya A., Juan E.;
RT "ADH and phylogenetic relationships of Drosophila lebanonesis
RT (Scaptodrosophila).";
RL J. Mol. Evol. 32:421-428(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
RX PubMed=9735295; DOI=10.1006/jmbi.1998.2015;
RA Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.;
RT "The refined crystal structure of Drosophila lebanonensis alcohol
RT dehydrogenase at 1.9-A resolution.";
RL J. Mol. Biol. 282:383-399(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH NAD AND PRODUCT.
RX PubMed=10366509; DOI=10.1006/jmbi.1999.2765;
RA Benach J., Atrian S., Gonzalez-Duarte R., Ladenstein R.;
RT "The catalytic reaction and inhibition mechanism of Drosophila alcohol
RT dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4-A
RT resolution by X-ray crystallography.";
RL J. Mol. Biol. 289:335-355(1999).
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. {ECO:0000269|PubMed:10366509}.
CC -!- INTERACTION:
CC P10807; P10807: Adh; NbExp=2; IntAct=EBI-7944097, EBI-7944097;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X53429; CAA37520.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X54814; CAA38583.1; -; Genomic_DNA.
DR EMBL; M97637; AAA28355.1; -; Genomic_DNA.
DR PIR; S12695; DEFFRL.
DR PDB; 1A4U; X-ray; 1.92 A; A/B=1-254.
DR PDB; 1B14; X-ray; 2.40 A; A/B=1-254.
DR PDB; 1B15; X-ray; 2.20 A; A/B=1-254.
DR PDB; 1B16; X-ray; 1.40 A; A/B=1-254.
DR PDB; 1B2L; X-ray; 1.60 A; A=1-254.
DR PDB; 1SBY; X-ray; 1.10 A; A/B=1-254.
DR PDB; 3RJ5; X-ray; 1.45 A; A/B=1-254.
DR PDB; 3RJ9; X-ray; 1.98 A; A/B/C/D/E/F=1-254.
DR PDBsum; 1A4U; -.
DR PDBsum; 1B14; -.
DR PDBsum; 1B15; -.
DR PDBsum; 1B16; -.
DR PDBsum; 1B2L; -.
DR PDBsum; 1SBY; -.
DR PDBsum; 3RJ5; -.
DR PDBsum; 3RJ9; -.
DR AlphaFoldDB; P10807; -.
DR SMR; P10807; -.
DR MINT; P10807; -.
DR iPTMnet; P10807; -.
DR FlyBase; FBgn0012438; Dleb\Adh.
DR SABIO-RK; P10807; -.
DR EvolutionaryTrace; P10807; -.
DR Proteomes; UP000504634; Unplaced.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000054471"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT BINDING 10..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10366509"
FT BINDING 138
FT /ligand="substrate"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2707261"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1SBY"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 149..172
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1SBY"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1SBY"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1SBY"
SQ SEQUENCE 254 AA; 27792 MW; 56DA3644E6B9CDCE CRC64;
MDLTNKNVIF VAALGGIGLD TSRELVKRNL KNFVILDRVE NPTALAELKA INPKVNITFH
TYDVTVPVAE SKKLLKKIFD QLKTVDILIN GAGILDDHQI ERTIAINFTG LVNTTTAILD
FWDKRKGGPG GIIANICSVT GFNAIHQVPV YSASKAAVVS FTNSLAKLAP ITGVTAYSIN
PGITRTPLVH TFNSWLDVEP RVAELLLSHP TQTSEQCGQN FVKAIEANKN GAIWKLDLGT
LEAIEWTKHW DSHI
