Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alcohol dehydrogenase class-3

Gene

ADH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Plays a central role in formaldehyde detoxification.1 Publication

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.2 Publications
A secondary alcohol + NAD+ = a ketone + NADH.2 Publications
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Kineticsi

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).1 Publication
  1. KM=1.4 µM for S-(hydroxymethyl)glutathione1 Publication
  2. KM=7 µM for S-hydroxymethylglutathione (at pH 8 and 25 degrees Celsius)1 Publication
  3. KM=7.7 µM for farnesol (at pH 7.5 and 25 degrees Celsius)1 Publication
  4. KM=22000 µM for cinnamylalcohol (at pH 7.5 and 25 degrees Celsius)1 Publication
  5. KM=3 µM for farnesol (at pH 10 and 25 degrees Celsius)1 Publication
  6. KM=800 µM for geraniol (at pH 10 and 25 degrees Celsius)1 Publication
  7. KM=3500 µM for cinnamylalcohol (at pH 10 and 25 degrees Celsius)1 Publication
  8. KM=4700 µM for 12-Hydroxydodecanoic acid (at pH 10 and 25 degrees Celsius)1 Publication
  1. Vmax=1.22 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Zinc 1; catalyticCombined sources1 Publication1
Binding sitei48NADCombined sources1 Publication1
Binding sitei49SubstrateBy similarity1
Metal bindingi69Zinc 1; catalyticCombined sources1 Publication1
Binding sitei69SubstrateBy similarity1
Metal bindingi70Zinc 1Combined sources1 Publication1
Metal bindingi99Zinc 2Combined sources1 Publication1
Metal bindingi102Zinc 2Combined sources1 Publication1
Metal bindingi105Zinc 2Combined sources1 Publication1
Metal bindingi113Zinc 2Combined sources1 Publication1
Metal bindingi177Zinc 1; catalyticCombined sources1 Publication1
Binding sitei226NADCombined sources1 Publication1
Binding sitei231NADCombined sources1 Publication1
Binding sitei272NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei372NADCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi202 – 207NADCombined sources1 Publication6
Nucleotide bindingi295 – 297NADCombined sources1 Publication3
Nucleotide bindingi320 – 322NADCombined sources1 Publication3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G43940-MONOMER
ReactomeiR-ATH-2161541 Abacavir metabolism
R-ATH-5365859 RA biosynthesis pathway
R-ATH-71384 Ethanol oxidation
SABIO-RKQ96533

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.12 Publications)
Alternative name(s):
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.-)
Short name:
FALDH
Short name:
FDH
Short name:
GSH-FDH
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.2842 Publications)
Gene namesi
Name:ADH2
Synonyms:ADHIII, FDH1
Ordered Locus Names:At5g43940
ORF Names:MRH10.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

AraportiAT5G43940

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001607712 – 379Alcohol dehydrogenase class-3Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ96533
PRIDEiQ96533

PTM databases

iPTMnetiQ96533

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Down-regulated by wounding and activated by salicylic acid (SA).1 Publication

Gene expression databases

ExpressionAtlasiQ96533 baseline and differential
GenevisibleiQ96533 AT

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi19667, 2 interactors
STRINGi3702.AT5G43940.2

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Beta strandi23 – 29Combined sources7
Beta strandi36 – 46Combined sources11
Helixi48 – 54Combined sources7
Beta strandi63 – 65Combined sources3
Beta strandi70 – 78Combined sources9
Beta strandi90 – 93Combined sources4
Beta strandi100 – 102Combined sources3
Helixi103 – 107Combined sources5
Helixi117 – 120Combined sources4
Turni121 – 123Combined sources3
Turni126 – 128Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi138 – 141Combined sources4
Turni144 – 146Combined sources3
Beta strandi149 – 156Combined sources8
Helixi157 – 159Combined sources3
Beta strandi160 – 162Combined sources3
Helixi169 – 172Combined sources4
Helixi173 – 176Combined sources4
Helixi178 – 187Combined sources10
Turni188 – 190Combined sources3
Beta strandi198 – 201Combined sources4
Helixi205 – 217Combined sources13
Beta strandi222 – 225Combined sources4
Helixi231 – 236Combined sources6
Turni237 – 239Combined sources3
Beta strandi242 – 244Combined sources3
Helixi246 – 248Combined sources3
Helixi253 – 260Combined sources8
Beta strandi265 – 270Combined sources6
Helixi275 – 283Combined sources9
Turni287 – 289Combined sources3
Beta strandi291 – 294Combined sources4
Beta strandi304 – 306Combined sources3
Helixi309 – 312Combined sources4
Beta strandi316 – 319Combined sources4
Helixi322 – 324Combined sources3
Helixi327 – 339Combined sources13
Helixi346 – 348Combined sources3
Beta strandi349 – 354Combined sources6
Helixi355 – 357Combined sources3
Helixi358 – 364Combined sources7
Beta strandi371 – 376Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UKOX-ray1.40A/B2-379[»]
4GL4X-ray1.80A/B2-379[»]
4JJIX-ray1.80A/B2-379[»]
4L0QX-ray1.95A/B2-379[»]
ProteinModelPortaliQ96533
SMRiQ96533
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022 Eukaryota
COG1062 LUCA
HOGENOMiHOG000294674
InParanoidiQ96533
KOiK00121
PhylomeDBiQ96533

Family and domain databases

CDDicd08300 alcohol_DH_class_III, 1 hit
InterProiView protein in InterPro
IPR014183 ADH_3
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SUPFAMiSSF50129 SSF50129, 2 hits
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR02818 adh_III_F_hyde, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q96533-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATQGQVITC KAAVAYEPNK PLVIEDVQVA PPQAGEVRIK ILYTALCHTD
60 70 80 90 100
AYTWSGKDPE GLFPCILGHE AAGIVESVGE GVTEVQAGDH VIPCYQAECR
110 120 130 140 150
ECKFCKSGKT NLCGKVRSAT GVGIMMNDRK SRFSVNGKPI YHFMGTSTFS
160 170 180 190 200
QYTVVHDVSV AKIDPTAPLD KVCLLGCGVP TGLGAVWNTA KVEPGSNVAI
210 220 230 240 250
FGLGTVGLAV AEGAKTAGAS RIIGIDIDSK KYETAKKFGV NEFVNPKDHD
260 270 280 290 300
KPIQEVIVDL TDGGVDYSFE CIGNVSVMRA ALECCHKGWG TSVIVGVAAS
310 320 330 340 350
GQEISTRPFQ LVTGRVWKGT AFGGFKSRTQ VPWLVEKYMN KEIKVDEYIT
360 370
HNLTLGEINK AFDLLHEGTC LRCVLDTSK
Length:379
Mass (Da):40,699
Last modified:March 27, 2002 - v2
Checksum:i045054298F16B258
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84E → G in AAB06322 (PubMed:9215914).Curated1
Sequence conflicti354T → S in CAA57973 (PubMed:8944774).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63931 Genomic DNA Translation: AAB06322.1
X82647 mRNA Translation: CAA57973.1
AB006703 Genomic DNA Translation: BAB09054.1
CP002688 Genomic DNA Translation: AED95034.1
AY039601 mRNA Translation: AAK62656.1
BT010169 mRNA Translation: AAQ22638.1
AK226412 mRNA Translation: BAE98557.1
AY087250 mRNA Translation: AAM64806.1
PIRiS71244
RefSeqiNP_199207.1, NM_123761.4 [Q96533-1]
UniGeneiAt.23457
At.63885

Genome annotation databases

EnsemblPlantsiAT5G43940.1; AT5G43940.1; AT5G43940 [Q96533-1]
GeneIDi834417
GrameneiAT5G43940.1; AT5G43940.1; AT5G43940 [Q96533-1]
KEGGiath:AT5G43940

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiADHX_ARATH
AccessioniPrimary (citable) accession number: Q96533
Secondary accession number(s): Q0WWE1, Q43384, Q9FND2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: April 25, 2018
This is version 157 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health