ID ADH1_PERMA Reviewed; 375 AA. AC P41680; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 28-JAN-2026, entry version 110. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase A subunit; GN Name=ADH1; Synonyms=ADH-1; 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 + NADH + H(+); 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 + NADH + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L15703; AAA40591.1; -; mRNA. DR PIR; A49107; A49107. DR AlphaFoldDB; P41680; -. DR SMR; P41680; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004745; F:all-trans-retinol dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042573; P:retinoic acid metabolic process; IEA:TreeGrafter. DR GO; GO:0042572; P:retinol metabolic process; IEA:TreeGrafter. DR CDD; cd08299; alcohol_DH_class_I_II_IV; 1. DR FunFam; 3.40.50.720:FF:000003; S-(hydroxymethyl)glutathione dehydrogenase; 1. DR FunFam; 3.90.180.10:FF:000001; S-(hydroxymethyl)glutathione dehydrogenase; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR020843; ER. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF1; ALCOHOL DEHYDROGENASE 1A; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P06757" FT CHAIN 2..375 FT /note="Alcohol dehydrogenase 1" FT /id="PRO_0000160667" 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 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 112 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" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P06757" FT MOD_RES 234 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P00329" FT MOD_RES 340 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P00329" SQ SEQUENCE 375 AA; 39834 MW; BA6878B0A071F901 CRC64; MSTAGKVIKC KAAVLWEPHK PFSIEDIEVA PPKAHEVRIK MVATGVCRSD DHVVSRSLAS PLPAVLGHEG AGIVESVGEG VTSVKPGDKV IPLFTPQCGK CRICKHPEYN LCMKNDLMQP RGTLLDGTSR FTCRGKAIHN FISTSTFSQY TVVDEMAVAK IDGASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVII GCKAAGAARI IAVDINKDKF AKAKELGATE CINPLDYSKP IQEVLQEMTD GGVDFSFEVI GRLDTMTSSL LSCHASCGVS VIVGVPPNAQ SLSVNPMSLL MGRSWKGAIF GGFKSKDSVP KLVTDFMAKK FPLEPLITHV LPFEKINEAF DLLRAGKSIR TVLTF //