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Protein

Alcohol dehydrogenase class-3

Gene

ADH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in formaldehyde detoxification.1 Publication

Catalytic activityi

An alcohol + NAD+ = an aldehyde or 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

Manual assertion based on experiment ini

  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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G43940-MONOMER.
ReactomeiR-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

TAIRiAT5G43940.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

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.
Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

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.
KEGGiath:AT5G43940.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi19667. 2 interactors.
STRINGi3702.AT5G43940.2.

PTM databases

iPTMnetiQ96533.

Proteomic databases

PaxDbiQ96533.
PRIDEiQ96533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT5G43940.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
InParanoidiQ96533.
KOiK00121.
PhylomeDBiQ96533.

Enzyme and pathway databases

BioCyciARA:AT5G43940-MONOMER.
ReactomeiR-ATH-71384. Ethanol oxidation.
SABIO-RKQ96533.

Miscellaneous databases

PROiQ96533.

Gene expression databases

ExpressionAtlasiQ96533. baseline and differential.
GenevisibleiQ96533. AT.

Family and domain databases

CDDicd08300. alcohol_DH_class_III. 1 hit.
Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADHX_ARATH
AccessioniPrimary (citable) accession number: Q96533
Secondary accession number(s): Q0WWE1, Q43384, Q9FND2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: November 30, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.