ADH_DROAN
ID ADH_DROAN Reviewed; 256 AA.
AC Q50L96; Q8N0A0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000250|UniProtKB:P00334};
DE EC=1.1.1.1;
GN Name=Adh {ECO:0000312|EMBL:BAD98197.1}; ORFNames=GF14888;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:BAD98197.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16143626; DOI=10.1534/genetics.105.041699;
RA Nozawa M., Aotsuka T., Tamura K.;
RT "A novel chimeric gene, siren, with retroposed promoter sequence in the
RT Drosophila bipectinata complex.";
RL Genetics 171:1719-1727(2005).
RN [2] {ECO:0000312|EMBL:ACF95828.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jones C.D., Shih H.-J.;
RT "Patterns of amino acid evolution in Drosophila ananassae chimeric gene,
RT siren, parallel those of other Adh derived chimeras.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:EDV30743.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000269|PubMed:17994087};
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 [4] {ECO:0000312|EMBL:AAM28691.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-145.
RX AGRICOLA=IND23292123;
RA Schawaroch V.A.;
RT "Phylogeny of a paradigm lineage: the Drosophila melanogaster species group
RT (Diptera: Drosophilidae).";
RL Biol. J. Linn. Soc. Lond. 76:21-37(2002).
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; AB194426; BAD98197.1; -; Genomic_DNA.
DR EMBL; EU877943; ACF95828.1; -; Genomic_DNA.
DR EMBL; CH902620; EDV30743.1; -; Genomic_DNA.
DR EMBL; AF459754; AAM28691.1; -; Genomic_DNA.
DR RefSeq; XP_001961522.1; XM_001961486.2.
DR AlphaFoldDB; Q50L96; -.
DR SMR; Q50L96; -.
DR STRING; 7217.FBpp0118080; -.
DR EnsemblMetazoa; FBtr0119588; FBpp0118080; FBgn0012113.
DR GeneID; 6492907; -.
DR KEGG; dan:6492907; -.
DR eggNOG; KOG4169; Eukaryota.
DR HOGENOM; CLU_010194_2_16_1; -.
DR InParanoid; Q50L96; -.
DR OMA; TTLQCAQ; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; Q50L96; -.
DR ChiTaRS; Adh; fly.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblMetazoa.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:EnsemblMetazoa.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0006117; P:acetaldehyde metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0046164; P:alcohol catabolic process; ISS:UniProtKB.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:EnsemblMetazoa.
DR GO; GO:0006069; P:ethanol oxidation; IEA:EnsemblMetazoa.
DR GO; GO:0006734; P:NADH metabolic process; IEA:EnsemblMetazoa.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT CHAIN 2..256
FT /note="Alcohol dehydrogenase"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT /id="PRO_0000352752"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00334,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 12..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00334"
SQ SEQUENCE 256 AA; 27854 MW; D9702C0DA79765E0 CRC64;
MALSLTNKNV VFVAGLGGIG LDTTKELLKR DLKNLVILDR IDNPVVIAEL KTINPKVTVT
FIPYDVTVPI TETKKLLKTI FDKLKTVDIL INGAGILDDH QIERTIAVNY TGLVNTTTAI
LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT
VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQSSQACG ENFVKAIELN QNGAIWKLDR
GTLEAIQWSK HWDSGI