ID   ADH2_CERCO              Reviewed;         258 AA.
AC   Q70UP5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
GN   Name=ADH2;
OS   Ceratitis cosyra (Mango fruit fly) (Trypeta cosyra).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratalaspis.
OX   NCBI_TaxID=194917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14562961; DOI=10.1007/s00239-003-2464-z;
RA   Goulielmos G.N., Loukas M., Bondinas G., Zouros E.;
RT   "Exploring the evolutionary history of the alcohol dehydrogenase gene (Adh)
RT   duplication in species of the family tephritidae.";
RL   J. Mol. Evol. 57:170-180(2003).
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; AJ539540; CAD62452.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70UP5; -.
DR   SMR; Q70UP5; -.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS: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   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..258
FT                   /note="Alcohol dehydrogenase 2"
FT                   /id="PRO_0000277839"
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;  28010 MW;  43B04144B00D107B CRC64;
     MGLSGKNVIF VGGLGFIGYE ACKQLMAKNM ASFFVFDVLD KPEDIKALQA LNPKTKVYYT
     KFDITSKQSI KSALADVVSK VKYIDALING AGILTDLNVE LTMNINLIGL INTTLEALPL
     MDKNKQGRGG VIVNIASVLG LEPCPPAAVY CASKFGVMGF SRSIGDPYYY NITGVAVVTF
     CPGLTETPLK NNIGSKYTFE YSKKISEELN NTKTQKPEVC GAHLAQVVES HENGGIYISN
     QGTLAKVTPT VYWQPTYH