Q96533 · ADHX_ARATH

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).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.4 μMS-(hydroxymethyl)glutathione
7 μMS-hydroxymethylglutathione825
7.7 μMfarnesol7.525
22000 μMcinnamylalcohol7.525
3 μMfarnesol1025
800 μMgeraniol1025
3500 μMcinnamylalcohol1025
4700 μM12-Hydroxydodecanoic acid1025
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.

TypeIDPosition(s)Description
Binding site47Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site48NAD+ (UniProtKB | ChEBI)
Binding site49an alcohol (UniProtKB | ChEBI)
Binding site69an alcohol (UniProtKB | ChEBI)
Binding site69Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site70Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site99Zn2+ 2 (UniProtKB | ChEBI)
Binding site102Zn2+ 2 (UniProtKB | ChEBI)
Binding site105Zn2+ 2 (UniProtKB | ChEBI)
Binding site113Zn2+ 2 (UniProtKB | ChEBI)
Binding site177Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site202-207NAD+ (UniProtKB | ChEBI)
Binding site226NAD+ (UniProtKB | ChEBI)
Binding site231NAD+ (UniProtKB | ChEBI)
Binding site272NAD+ (UniProtKB | ChEBI)
Binding site295-297NAD+ (UniProtKB | ChEBI)
Binding site320-322NAD+ (UniProtKB | ChEBI)
Binding site372NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalcohol dehydrogenase (NAD+) activity
Molecular FunctionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Molecular FunctionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
Molecular FunctionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
Molecular FunctionS-nitrosoglutathione reductase (NADH) activity
Molecular Functionzinc ion binding
Biological Processformaldehyde catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alcohol dehydrogenase class-3
  • EC number
  • Alternative names
    • Alcohol dehydrogenase class-III
    • Glutathione-dependent formaldehyde dehydrogenase
      (FALDH
      ; FDH
      ; GSH-FDH
      ) (EC:1.1.1.-) . EC:1.1.1.- (UniProtKB | ENZYME | Rhea)
    • Nitrosoglutathione reductase
      (EC:1.1.1.-
      ) . EC:1.1.1.- (UniProtKB | ENZYME | Rhea)
    • S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284
      ) . EC:1.1.1.284 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      ADH2
    • Synonyms
      ADHIII
      , FDH1
      , GSNOR
    • ORF names
      MRH10.4
    • Ordered locus names
      At5g43940

Organism names

  • Taxonomic identifier
  • Strains
    • cv. C24
    • cv. Landsberg erecta
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q96533
  • Secondary accessions
    • Q0WWE1
    • Q43384
    • Q9FND2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001607712-379Alcohol dehydrogenase class-3

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Induction

Down-regulated by wounding and activated by salicylic acid (SA).

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

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.

  • Length
    379
  • Mass (Da)
    40,699
  • Last updated
    2002-03-27 v2
  • Checksum
    045054298F16B258
MATQGQVITCKAAVAYEPNKPLVIEDVQVAPPQAGEVRIKILYTALCHTDAYTWSGKDPEGLFPCILGHEAAGIVESVGEGVTEVQAGDHVIPCYQAECRECKFCKSGKTNLCGKVRSATGVGIMMNDRKSRFSVNGKPIYHFMGTSTFSQYTVVHDVSVAKIDPTAPLDKVCLLGCGVPTGLGAVWNTAKVEPGSNVAIFGLGTVGLAVAEGAKTAGASRIIGIDIDSKKYETAKKFGVNEFVNPKDHDKPIQEVIVDLTDGGVDYSFECIGNVSVMRAALECCHKGWGTSVIVGVAASGQEISTRPFQLVTGRVWKGTAFGGFKSRTQVPWLVEKYMNKEIKVDEYITHNLTLGEINKAFDLLHEGTCLRCVLDTSK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4K7D6F4K7D6_ARATHHOT5391

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict84in Ref. 1; AAB06322
Sequence conflict354in Ref. 2; CAA57973

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp