Q96533 · ADHX_ARATH
- ProteinAlcohol dehydrogenase class-3
- GeneADH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Alcohol dehydrogenase catalyzing the reduction of nitrosoglutathione (PubMed:38308388).
Can also use long-chain alcohols including cinnamyl alcohol and geraniol, and, to a lower extent, octanol (PubMed:38308388).
Plays a central role in formaldehyde detoxification (PubMed:12913179).
Not able to use ethanol (EtOH) as substrate (PubMed:38308388).
Can also use long-chain alcohols including cinnamyl alcohol and geraniol, and, to a lower extent, octanol (PubMed:38308388).
Plays a central role in formaldehyde detoxification (PubMed:12913179).
Not able to use ethanol (EtOH) as substrate (PubMed:38308388).
Catalytic activity
- a primary alcohol + NAD+ = an aldehyde + NADH + H+
- S-nitrosoglutathione + NADH + H+ = S-(hydroxysulfenamide)glutathione + NAD+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Repressed by thiol-modifying agents N-ethylmaleimide (NEM) and 5,5-dithio-bis-(2-nitrobenzoic acid) (DTNB), as well as by methyl methanethiosulfonate (MMTS) in a dose-dependent manner (PubMed:38308388).
Inhibited by hydrogen peroxide H2O2 (PubMed:38308388).
Inhibited by hydrogen peroxide H2O2 (PubMed:38308388).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.4 μM | S-(hydroxymethyl)glutathione | |||||
7 μM | S-hydroxymethylglutathione | 8 | 25 | |||
7.7 μM | farnesol | 7.5 | 25 | |||
22000 μM | cinnamylalcohol | 7.5 | 25 | |||
3 μM | farnesol | 10 | 25 | |||
800 μM | geraniol | 10 | 25 | |||
3500 μM | cinnamylalcohol | 10 | 25 | |||
4700 μM | 12-Hydroxydodecanoic acid | 10 | 25 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.22 μmol/min/mg |
kcat is 1351 min-1 with S-hydroxymethylglutathione as substrate (at pH 8 and 25 degrees Celsius). kcat is 6 min-1 with farnesol as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 324 min-1 with cinnamylalcohol as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 126 min-1 with farnesol as substrate (at pH 10 and 25 degrees Celsius). kcat is 1200 min-1 with geraniol as substrate (at pH 10 and 25 degrees Celsius). kcat is 1220 min-1 with cinnamylalcohol as substrate (at pH 10 and 25 degrees Celsius). kcat is 335 min-1 with 12-Hydroxydodecanoic acid as substrate (at pH 10 and 25 degrees Celsius).
pH Dependence
Optimum pH is 7.9-9.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 48 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 49 | an alcohol (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 69 | an alcohol (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 69 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 70 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 99 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 102 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 105 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 113 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 177 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 202-207 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GLGTVG | ||||||
Binding site | 226 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 231 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 272 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 295-297 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VGV | ||||||
Binding site | 320-322 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TAF | ||||||
Binding site | 372 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | alcohol dehydrogenase (NAD+) activity | |
Molecular Function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity | |
Molecular Function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity | |
Molecular Function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity | |
Molecular Function | S-nitrosoglutathione reductase (NADH) activity | |
Molecular Function | zinc ion binding | |
Biological Process | formaldehyde catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlcohol dehydrogenase class-3
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ96533
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000160771 | 2-379 | Alcohol dehydrogenase class-3 | |||
Sequence: ATQGQVITCKAAVAYEPNKPLVIEDVQVAPPQAGEVRIKILYTALCHTDAYTWSGKDPEGLFPCILGHEAAGIVESVGEGVTEVQAGDHVIPCYQAECRECKFCKSGKTNLCGKVRSATGVGIMMNDRKSRFSVNGKPIYHFMGTSTFSQYTVVHDVSVAKIDPTAPLDKVCLLGCGVPTGLGAVWNTAKVEPGSNVAIFGLGTVGLAVAEGAKTAGASRIIGIDIDSKKYETAKKFGVNEFVNPKDHDKPIQEVIVDLTDGGVDYSFECIGNVSVMRAALECCHKGWGTSVIVGVAASGQEISTRPFQLVTGRVWKGTAFGGFKSRTQVPWLVEKYMNKEIKVDEYITHNLTLGEINKAFDLLHEGTCLRCVLDTSK |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Induction
Down-regulated by wounding and activated by salicylic acid (SA).
Gene expression databases
Structure
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q96533-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length379
- Mass (Da)40,699
- Last updated2002-03-27 v2
- Checksum045054298F16B258
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4K7D6 | F4K7D6_ARATH | HOT5 | 391 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 84 | in Ref. 1; AAB06322 | ||||
Sequence: E → G | ||||||
Sequence conflict | 354 | in Ref. 2; CAA57973 | ||||
Sequence: T → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U63931 EMBL· GenBank· DDBJ | AAB06322.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X82647 EMBL· GenBank· DDBJ | CAA57973.1 EMBL· GenBank· DDBJ | mRNA | ||
AB006703 EMBL· GenBank· DDBJ | BAB09054.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED95034.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY039601 EMBL· GenBank· DDBJ | AAK62656.1 EMBL· GenBank· DDBJ | mRNA | ||
BT010169 EMBL· GenBank· DDBJ | AAQ22638.1 EMBL· GenBank· DDBJ | mRNA | ||
AK226412 EMBL· GenBank· DDBJ | BAE98557.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087250 EMBL· GenBank· DDBJ | AAM64806.1 EMBL· GenBank· DDBJ | mRNA |