ADH_DROVI
ID ADH_DROVI Reviewed; 254 AA.
AC B4M8Y0; O96996; Q27431; Q9U8P1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=Adh1 {ECO:0000312|EMBL:EDW57656.1};
GN Synonyms=Adh-1 {ECO:0000312|EMBL:AAB02632.1}; ORFNames=GJ18208;
GN and
GN Name=Adh2 {ECO:0000312|EMBL:EDW57657.1};
GN Synonyms=Adh-2 {ECO:0000312|EMBL:AAB02633.1}; ORFNames=GJ18209;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB02632.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ADH1 AND ADH2).
RX PubMed=8583887; DOI=10.1093/oxfordjournals.molbev.a025551;
RA Nurminsky D.I., Moriyama E.N., Lozovskaya E.R., Hartl D.L.;
RT "Molecular phylogeny and genome evolution in the Drosophila virilis species
RT group: duplications of the alcohol dehydrogenase gene.";
RL Mol. Biol. Evol. 13:132-149(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:EDW57656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ADH1 AND ADH2).
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW57656.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABG56040.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-248 (ADH1).
RC STRAIN=174 {ECO:0000312|EMBL:ABG56040.1};
RX PubMed=16678448; DOI=10.1016/j.ympev.2006.03.026;
RA Wang B.-C., Park J., Watabe H.-A., Gao J.-J., Xiangyu J.G., Aotsuka T.,
RA Chen H.-W., Zhang Y.-P.;
RT "Molecular phylogeny of the Drosophila virilis section (Diptera:
RT Drosophilidae) based on mitochondrial and nuclear sequences.";
RL Mol. Phylogenet. Evol. 40:484-500(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAA85906.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-248 (ADH1).
RA Katoh T., Tamura K., Aotsuka T.;
RT "Origin of Hawaiian drosophilids inferred from alcohol dehydrogenase gene
RT sequences.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAA06663.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-165.
RX PubMed=10093214; DOI=10.1007/pl00006468;
RA Atrian S., Gonzalez-Duarte R.;
RT "The Drosophila virilis alcohol dehydrogenase catalytic residues are
RT conserved.";
RL J. Mol. Evol. 48:262-263(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, 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}.
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DR EMBL; U26846; AAB02632.1; -; Genomic_DNA.
DR EMBL; U26846; AAB02633.1; -; Genomic_DNA.
DR EMBL; CH940654; EDW57656.1; -; Genomic_DNA.
DR EMBL; CH940654; EDW57657.1; -; Genomic_DNA.
DR EMBL; DQ471643; ABG56040.1; -; Genomic_DNA.
DR EMBL; DQ471668; ABG56065.1; -; Genomic_DNA.
DR EMBL; AB033640; BAA85906.1; -; mRNA.
DR EMBL; AJ005667; CAA06663.1; -; Genomic_DNA.
DR RefSeq; XP_002057583.1; XM_002057547.2.
DR RefSeq; XP_002057584.1; XM_002057548.2.
DR AlphaFoldDB; B4M8Y0; -.
DR SMR; B4M8Y0; -.
DR STRING; 7244.FBpp0232625; -.
DR EnsemblMetazoa; FBtr0234133; FBpp0232625; FBgn0014836.
DR EnsemblMetazoa; FBtr0234134; FBpp0232626; FBgn0014837.
DR GeneID; 6633890; -.
DR GeneID; 6634390; -.
DR KEGG; dvi:6633890; -.
DR KEGG; dvi:6634390; -.
DR eggNOG; KOG4169; Eukaryota.
DR HOGENOM; CLU_010194_2_16_1; -.
DR InParanoid; B4M8Y0; -.
DR OMA; TTLQCAQ; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; B4M8Y0; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
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 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT CHAIN 2..254
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000355576"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00334,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT CONFLICT 140
FT /note="T -> S (in Ref. 1; AAB02632/AAB02633)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="K -> E (in Ref. 1; AAB02632/AAB02633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27608 MW; 176D48D05518DF17 CRC64;
MAIANKNIIF VAGLGGIGLD TSREIVKSGP KNLVILDRIE NPTAIAELKA INPKVTVTFY
PYDVTVPVAE TTKLLKTIFA KLKTVDLLIN GAGILDDHQI ERTIAVNFTG TVNTTTAIME
FWDKRKGGPG GVIANICSVT GFNAIYQVPV YSASKAAALS FTNSLARLAP ITGVTAYSIN
PGITRTPLVH KFNSWLDVEP RVGELLLEHP TQTTLECAQN FVKAIEANQN GAIWQLDLGR
LISVEWTKHW DSHI
