ADH2_SOLLC
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 03-AUG-2022, entry version 122.
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 + 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 Evidence={ECO:0000250|UniProtKB:P06525};
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 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}.
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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.Solyc06g059740.2.1; -.
DR PaxDb; P28032; -.
DR GeneID; 544074; -.
DR KEGG; sly:544074; -.
DR eggNOG; KOG0022; Eukaryota.
DR InParanoid; P28032; -.
DR OrthoDB; 664798at2759; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P28032; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
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 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; 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="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 50
FT /ligand="substrate"
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="substrate"
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
