ID   ADH_BACOL               Reviewed;         258 AA.
AC   Q9NAR7; P82461;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alcohol dehydrogenase;
DE            EC=1.1.1.1;
GN   Name=ADH;
OS   Bactrocera oleae (Olive fruit fly) (Dacus oleae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Bactrocera; Daculus.
OX   NCBI_TaxID=104688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10732677; DOI=10.1007/pl00008679;
RA   Benos P., Tavernarakis N., Brogna S., Thireos G., Savakis C.;
RT   "Acquisition of a potential marker for insect transformation: isolation of
RT   a novel alcohol dehydrogenase gene from Bactrocera oleae by functional
RT   complementation in yeast.";
RL   Mol. Gen. Genet. 263:90-95(2000).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AJ250007; CAB94710.1; -; mRNA.
DR   RefSeq; NP_001302558.1; NM_001315629.1.
DR   AlphaFoldDB; Q9NAR7; -.
DR   SMR; Q9NAR7; -.
DR   GeneID; 106621041; -.
DR   KEGG; bod:106621041; -.
DR   OrthoDB; 1053465at2759; -.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   InterPro; IPR002426; ADH_Ceratitis-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; PR01169; CERATITISADH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..258
FT                   /note="Alcohol dehydrogenase"
FT                   /id="PRO_0000054450"
FT   ACT_SITE        150
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   258 AA;  27830 MW;  033592FD0968EADB CRC64;
     MGLSGKNVVF VGGLGFIGYE ACKQIMTKNV ASFFVFDVLE NAENIKALQA INPKTKVYYT
     KFDITNKASI KSAFADVIAK VQYIDVLVNG AGILTDPNVE LTMNINLIGL INTTLEAIPL
     MDKNKKGRGG LIVNIASVLG LEPAPPAAIY CASKFGVMGF SRSISDPYYY NLTGIAVATF
     CPGLTETPLK NNIATKYTFE YSKVIGDKLN NTKTQKPEAC GAHLAQVLDT AENGGIYISN
     QGTLSKVTPT VYWQPTFN