ID   ADH6_PERMA              Reviewed;         375 AA.
AC   P41681;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alcohol dehydrogenase 6;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase 2;
DE            Short=ADH-2;
GN   Name=ADH6;
OS   Peromyscus maniculatus (North American deer mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Peromyscus.
OX   NCBI_TaxID=10042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8227055; DOI=10.1016/s0021-9258(19)74554-2;
RA   Zheng Y.W., Bey M., Liu H., Felder M.R.;
RT   "Molecular basis of the alcohol dehydrogenase-negative deer mouse. Evidence
RT   for deletion of the gene for class I enzyme and identification of a
RT   possible new enzyme class.";
RL   J. Biol. Chem. 268:24933-24939(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-V subfamily. {ECO:0000305}.
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DR   EMBL; L15704; AAA40592.1; -; mRNA.
DR   PIR; B49107; B49107.
DR   AlphaFoldDB; P41681; -.
DR   SMR; P41681; -.
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; IPR028633; ADH6.
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   PANTHER; PTHR43880:SF20; PTHR43880:SF20; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..375
FT                   /note="Alcohol dehydrogenase 6"
FT                   /id="PRO_0000160689"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   375 AA;  39828 MW;  F0194982C94DE279 CRC64;
     MSTAGKVIRC KAAVLWKPGA PLTMEEIDVA PPKGKEVRVK MVAAGICGTD IKSLDNKKLA
     PFCPIIMGHE GTGIVESVGE GVSTVKTGDK VIILCLPQCG ECNTCLNSKN NICKEVRLSG
     THLTSEGNSR ITCKGKTTYQ YITTGTFSEY IVIKEISVAK VDEDALLEKA CIIGCGFATG
     FGAAINSAKV SPGSTCAVFG LGGVGLSVIM GCKAAGAARI IAVDTNKDKF AKAKTVGATE
     CIDPQDFEKP IQQVLFDMMN DGADFTFEVT GNPETVETAL ASCHKDHGVC VIVGSLASWI
     QLNINSHLFF SGRTLKGSVL GGWKTKEEIP KLVSDYTAKK FNLDPLITHT LTLDKVNEAI
     QLMKNGQCIR CVLLP