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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.1 Publication
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.1 Publication

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Kineticsi

  1. KM=1.4 µM for S-(hydroxymethyl)glutathione
  1. Vmax=1.22 µmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Zinc 1; catalyticBy similarity
Metal bindingi69 – 691Zinc 1; catalyticBy similarity
Metal bindingi99 – 991Zinc 2By similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi105 – 1051Zinc 2By similarity
Metal bindingi113 – 1131Zinc 2By similarity
Metal bindingi177 – 1771Zinc 1; catalyticBy similarity

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.
ARA:GQT-1380-MONOMER.
ReactomeiREACT_296764. Abacavir metabolism.
REACT_311425. RA biosynthesis pathway.
REACT_319123. Ethanol oxidation.
SABIO-RKQ96533.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
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:1.1.1.284)
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
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G43940.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 379378Alcohol dehydrogenase class-3PRO_0000160771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ96533.
PRIDEiQ96533.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

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

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi19667. 2 interactions.
STRINGi3702.AT5G43940.2.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Beta strandi23 – 297Combined sources
Beta strandi36 – 4611Combined sources
Helixi48 – 547Combined sources
Beta strandi63 – 653Combined sources
Beta strandi70 – 789Combined sources
Beta strandi90 – 934Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 1075Combined sources
Helixi117 – 1204Combined sources
Turni121 – 1233Combined sources
Turni126 – 1283Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi138 – 1414Combined sources
Turni144 – 1463Combined sources
Beta strandi149 – 1568Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1623Combined sources
Helixi169 – 1724Combined sources
Helixi173 – 1764Combined sources
Helixi178 – 18710Combined sources
Turni188 – 1903Combined sources
Beta strandi198 – 2014Combined sources
Helixi205 – 21713Combined sources
Beta strandi222 – 2254Combined sources
Helixi231 – 2366Combined sources
Turni237 – 2393Combined sources
Beta strandi242 – 2443Combined sources
Helixi246 – 2483Combined sources
Helixi253 – 2608Combined sources
Beta strandi265 – 2706Combined sources
Helixi275 – 2839Combined sources
Turni287 – 2893Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi304 – 3063Combined sources
Helixi309 – 3124Combined sources
Beta strandi316 – 3194Combined sources
Helixi322 – 3243Combined sources
Helixi327 – 33913Combined sources
Helixi346 – 3483Combined sources
Beta strandi349 – 3546Combined sources
Helixi355 – 3573Combined sources
Helixi358 – 3647Combined sources
Beta strandi371 – 3766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
InParanoidiQ96533.
KOiK00121.
PhylomeDBiQ96533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841E → G in AAB06322 (PubMed:9215914).Curated
Sequence conflicti354 – 3541T → S in CAA57973 (PubMed:8944774).Curated

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_123761.3. [Q96533-1]
UniGeneiAt.23457.
At.63885.

Genome annotation databases

EnsemblPlantsiAT5G43940.1; AT5G43940.1; AT5G43940. [Q96533-1]
GeneIDi834417.
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_123761.3. [Q96533-1]
UniGeneiAt.23457.
At.63885.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19667. 2 interactions.
STRINGi3702.AT5G43940.2.

Proteomic databases

PaxDbiQ96533.
PRIDEiQ96533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT5G43940.

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
InParanoidiQ96533.
KOiK00121.
PhylomeDBiQ96533.

Enzyme and pathway databases

BioCyciARA:AT5G43940-MONOMER.
ARA:GQT-1380-MONOMER.
ReactomeiREACT_296764. Abacavir metabolism.
REACT_311425. RA biosynthesis pathway.
REACT_319123. Ethanol oxidation.
SABIO-RKQ96533.

Miscellaneous databases

PROiQ96533.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the Arabidopsis and rice formaldehyde dehydrogenase genes: implications for the origin of plant ADH enzymes."
    Dolferus R., Osterman J.C., Peacock W.J., Dennis E.S.
    Genetics 146:1131-1141(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. C24.
  2. "Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class P and liver class I alcohol dehydrogenases."
    Martinez M.C., Achkor H., Persson B., Fernandez M.R., Shafqat J., Farres J., Joernvall H., Pares X.
    Eur. J. Biochem. 241:849-857(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ENZYME ACTIVITY.
    Strain: cv. Landsberg erecta.
    Tissue: Flower.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
    Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "The gene encoding glutathione-dependent formaldehyde dehydrogenase/GSNO reductase is responsive to wounding, jasmonic acid and salicylic acid."
    Diaz M., Achkor H., Titarenko E., Martinez M.C.
    FEBS Lett. 543:136-139(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis."
    Achkor H., Diaz M., Fernandez M.R., Biosca J.A., Pares X., Martinez M.C.
    Plant Physiol. 132:2248-2255(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

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: June 24, 2015
This is version 135 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

External Data

Dasty 3

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 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.