ID   ADH1_COTJA              Reviewed;         375 AA.
AC   P19631;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=ADH3;
DE   AltName: Full=Alcohol dehydrogenase subunit alpha;
GN   Name=ADH1;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   TISSUE=Liver;
RX   PubMed=2252897; DOI=10.1021/bi00488a024;
RA   Kaiser R., Nussrallah B., Dam R., Wagner F.W., Joernvall H.;
RT   "Avian alcohol dehydrogenase. Characterization of the quail enzyme,
RT   functional interpretations, and relationships to the different classes of
RT   mammalian alcohol dehydrogenase.";
RL   Biochemistry 29:8365-8371(1990).
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   -!- 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-I subfamily. {ECO:0000305}.
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DR   PIR; A35837; A35837.
DR   AlphaFoldDB; P19631; -.
DR   SMR; P19631; -.
DR   iPTMnet; P19631; -.
DR   SABIO-RK; P19631; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..375
FT                   /note="Alcohol dehydrogenase 1"
FT                   /id="PRO_0000160673"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   BINDING         200..205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         293..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2252897"
SQ   SEQUENCE   375 AA;  39808 MW;  61DA4EA003DEEF7A CRC64;
     STAGKVIKCK AAVLWEANKP FSLEEVEVAP PKAHEVRIKI VATGICRSDD HVVTGALAMP
     FPVILGHEAA GVVESVGEKV TLLKPGDAVI PLFVPQCGEC RSCLSTKGNL CIKNDLSSSP
     TGLMADGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAAAK IDSAAPLEKV CLIGCGFSTG
     YGAVLQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATE
     CVNPKDFKKP IHEVLTEMTG KGVDYSFEVI GRIETMTEAL ASCHYNYGVS VIVGVPPAAQ
     KISFDPMLIF SGRTWKGSVF GGWKSKDAVP KLVADYMKKK FVLDPLITHT LPFTKINEGF
     DLLRTGKSIR TVLVL