ID   ADH1_ALLMI              Reviewed;         374 AA.
AC   P80222;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase, major;
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   TISSUE=Liver;
RX   PubMed=8365416; DOI=10.1111/j.1432-1033.1993.tb18115.x;
RA   Persson B., Bergman T., Keung W.M., Waldenstroem U., Holmquist B.,
RA   Vallee B.L., Joernvall H.;
RT   "Basic features of class-I alcohol dehydrogenase: variable and constant
RT   segments coordinated by inter-class and intra-class variability.
RT   Conclusions from characterization of the alligator enzyme.";
RL   Eur. J. Biochem. 216:49-56(1993).
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; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
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; S35669; S35669.
DR   AlphaFoldDB; P80222; -.
DR   SMR; P80222; -.
DR   STRING; 8496.XP_006264567.1; -.
DR   iPTMnet; P80222; -.
DR   eggNOG; KOG0022; Eukaryota.
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; Zinc.
FT   CHAIN           1..374
FT                   /note="Alcohol dehydrogenase 1"
FT                   /id="PRO_0000160675"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         292..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
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:8365416"
FT   VARIANT         186
FT                   /note="D -> T"
FT   VARIANT         317
FT                   /note="S -> T"
SQ   SEQUENCE   374 AA;  39670 MW;  384BCB2D36E2FA32 CRC64;
     STAGKVIKCK AAITWEIKKP FSIEEIEVAP PKAHEVRIKI LATGICRSDD HVTAGLLTMP
     LPMILGHEAA GVVESTGEGV TSLKPGDKVI PLFVPQCGEC MPCLKSNGNL CIRNDLGSPS
     GLMADGTSRF TCKGKDIHHF IGTSTFTEYT VVHETAVARI DAAAPLEKVC LIGCGFSTGY
     GAAVKDAKVE PGSTCAVFGL GGVGLSTIMG CKAAGASRII GIDINKDKFA KAKELGATEC
     INPLDCKKPI QEVLSEMTGG GVDYSFEVIG RIDTMTAALA CCQDNYGTSV IVGVPPASEK
     ITFNPMMLFT GRTWKGSVFG GWKSKESVPK LVADYMEKKI NLDGLITHTL PFDKINEGFE
     LLRTGKSIRS VLTF