ID ADH2_SOLLC Reviewed; 380 AA. AC P28032; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 02-SEP-2026, entry version 136. DE RecName: Full=Alcohol dehydrogenase 2; DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525}; GN Name=ADH2; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; OC Solanum subgen. Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=8428654; DOI=10.1016/0378-1119(93)90119-n; RA Genez A.L., Staraci L.C., Alexander D.C., Rejda V.M., Williamson V.M., RA Chase T. Jr., Williams B.G.; RT "Isolation of a tomato alcohol dehydrogenase 2-encoding cDNA using phage- RT promoted antibody screening of a plasmid cDNA library."; RL Gene 123:157-164(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. De Ruiter 83G38; RX PubMed=7811967; DOI=10.1007/bf00040690; RA Longhurst T., Lee E., Hinde R., Brady C., Speirs J.; RT "Structure of the tomato Adh2 gene and Adh2 pseudogenes, and a study of RT Adh2 gene expression in fruit."; RL Plant Mol. Biol. 26:1073-1084(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 252-380. RC STRAIN=cv. Orlando; RX PubMed=1765164; DOI=10.1016/0014-5793(91)81379-m; RA van der Straeten D., Pousada R.A.R., Gielen J., van Montagu M.; RT "Tomato alcohol dehydrogenase. Expression during fruit ripening and under RT hypoxic conditions."; RL FEBS Lett. 295:39-42(1991). 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 (By similarity). Homotetramer. CC {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; M86724; AAA34133.1; -; mRNA. DR EMBL; X77233; CAA54450.1; -; Genomic_DNA. DR EMBL; X60600; CAA43055.1; -; mRNA. DR PIR; S51826; S51826. DR RefSeq; NP_001234099.1; NM_001247170.2. DR AlphaFoldDB; P28032; -. DR SMR; P28032; -. DR STRING; 4081.P28032; -. DR PaxDb; 4081-P28032; -. DR GeneID; 544074; -. DR KEGG; sly:544074; -. DR eggNOG; KOG0022; Eukaryota. DR InParanoid; P28032; -. DR OrthoDB; 417550at2759; -. DR Proteomes; UP000004994; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central. 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:SF40; ALCOHOL DEHYDROGENASE 2; 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; Reference proteome; Zinc. FT CHAIN 1..380 FT /note="Alcohol dehydrogenase 2" FT /id="PRO_0000160702" 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 323 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; 41040 MW; D5B123DF9DE28027 CRC64; MSTTVGQVIR CKAAVAWEAG KPLVMEEVDV APPQKMEVRL KILYTSLCHT DVYFWEAKGQ NPVFPRILGH EAAGIVESVG EGVTDLAPGD HVLPVFTGEC KDCAHCKSEE SNMCSLLRIN TDRGVMLNDG KSRFSINGNP IYHFVGTSTF SEYTVVHVGC VAKINPLAPL DKVCVLSCGI STGLGASLNV AKPTKGSSVA IFGLGAVGLA AAEGARIAGA SRIIGVDLNA SRFEQAKKFG VTEFVNPKDY SKPVQEVIAE MTDGGVDRSV ECTGHIDAMI SAFECVHDGW GVAVLVGVPH KEAVFKTHPL NFLNERTLKG TFFGNYKPRS DIPCVVEKYM NKELELEKFI THTLPFAEIN KAFDLMLKGE GLRCIITMAD //