ID ADH1_APTAU Reviewed; 375 AA. AC P49645; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 114. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase I; GN Name=ADH1; OS Apteryx australis (Southern brown kiwi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Apterygiformes; Apterygidae; Apteryx. OX NCBI_TaxID=8822; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=7541757; DOI=10.1016/0014-5793(95)00554-m; RA Hjelmqvist L., Metsis M., Persson H., Hoeoeg J.-O., McLennan J., RA Joernvall H.; RT "Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in RT separate vertebrate lines, and correlation with 12S rRNA patterns."; RL FEBS Lett. 367:306-310(1995). RN [2] RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-2. RX PubMed=7607314; DOI=10.1016/0014-5793(95)00572-q; RA Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J., RA Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.; RT "Multiplicity of N-terminal structures of medium-chain alcohol RT dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and RT higher vertebrate class I, II, and III forms of the enzyme."; RL FEBS Lett. 367:237-240(1995). 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 -!- SUBUNIT: Homodimer. 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; S78778; AAC60755.2; -; mRNA. DR PIR; S66272; S66272. DR AlphaFoldDB; P49645; -. DR SMR; P49645; -. DR iPTMnet; P49645; -. 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:001857; Alcohol dehydrogenase class 4 mu/sigma chain; 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 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; KW Oxidoreductase; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..375 FT /note="Alcohol dehydrogenase 1" FT /id="PRO_0000160671" 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:0000269|PubMed:7607314" SQ SEQUENCE 375 AA; 39631 MW; A6EBC1BEB0D66E02 CRC64; MSTAGKVIKC KAAVLWEPKK PFSIEEVEVA PPKAHEVRIK ILATGICRSD DHVITGALVR PFPIILGHEA AGVVESVGEG VTSVKPGDKV IPLFVPQCGE CSACLSTKGN LCSKNDIGSA SGLMPDGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAVAK IAAAAPLEKV CLIGCGFSTG YGAAVQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATD CVNPKDFTKP IHEVLMEMTG LGVDYSFEVI GHTETMAAAL ASCHFNYGVS VILGVPPAAE KISFDPMLLF SGRTWKGSVF GGWKSKDAVP KLVADYMEKK FVLEPLITHT LPFIKINEGF DLLRKGKSIR SVLVF //