ID ADH1_TRIRP Reviewed; 380 AA. AC P13603; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 02-SEP-2026, entry version 120. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525}; GN Name=ADH1; OS Trifolium repens (Creeping white clover). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium. OX NCBI_TaxID=3899; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Huia; RX PubMed=2395651; DOI=10.1093/nar/18.16.4913; RA Ellison N.W., Yu P.L., White D.W.R.; RT "Nucleotide sequence of a white clover alcohol dehydrogenase cDNA."; RL Nucleic Acids Res. 18:4913-4913(1990). 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 Evidence={ECO:0000250|UniProtKB:P06525}; 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 Evidence={ECO:0000250|UniProtKB:P06525}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P06525}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06525}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {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; X14826; CAA32934.1; -; mRNA. DR PIR; S14680; DEJYAW. DR AlphaFoldDB; P13603; -. DR SMR; P13603; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:TreeGrafter. DR CDD; cd08301; alcohol_DH_plants; 1. DR FunFam; 3.90.180.10:FF:000067; alcohol dehydrogenase 1-like isoform X1; 1. DR FunFam; 3.40.50.720:FF:001292; Alcohol dehydrogenase class-P; 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; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF26; ALCOHOL DEHYDROGENASE CLASS-P; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 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 Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1..380 FT /note="Alcohol dehydrogenase 1" FT /id="PRO_0000160715" FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 50 FT /ligand="an alcohol" FT /ligand_id="ChEBI:CHEBI:30879" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 50 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 70 FT /ligand="an alcohol" FT /ligand_id="ChEBI:CHEBI:30879" FT /evidence="ECO:0000250|UniProtKB:P00327" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 203..208 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 227 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 232 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 273 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 296..298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P00327" FT BINDING 296 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 373 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P06525" SQ SEQUENCE 380 AA; 41172 MW; 6C6E805FC3ABA663 CRC64; MSNTAGQVIK CRAAVAWEAG KPLVIEEVEV APPQAGEVRL KILFTSLCHT DVYFWEAKGQ TPLFPRIFGH EAGGIVESVG EGVTHLKPGD HALPVFTGEC GECPHCKSEE SNMCNLLRIN TDRGVMINDN KSRFSIKGQP VHHFVGTSTF SEYTVVHAGC VAKINPDAPL DKVCILSCGI CTGLGATVNV AKPKPGSSVA IFGLGAVGLA AAEGARMSGA SRIIGVDLVS SRFELAKKFG VNEFVNPKDH DKPVQQVIAE MTDGGVDRAV ECTGSIQAMI SAFECVHDGW GVAVLVGVPK KDDAFKTHPM NFLNERTLKG TFYGNYKPRT DLPNVVEQYM KGELELEKFI THSIPFSEIN KAFDYMLKGE SIRCIIRMEE //