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Q96533 (ADHX_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase class-3

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
Short name=GSH-FDH
EC=1.1.1.-
S-(hydroxymethyl)glutathione dehydrogenase
EC=1.1.1.284
Gene names
Name:ADH2
Synonyms:ADHIII, FDH1
Ordered Locus Names:At5g43940
ORF Names:MRH10.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a central role in formaldehyde detoxification. Ref.9

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH. Ref.2

S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H. Ref.2

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Tissue specificity

Ubiquitous. Ref.2

Induction

Down-regulated by wounding and activated by salicylic acid (SA). Ref.8

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=1.4 µM for S-(hydroxymethyl)glutathione

Vmax=1.22 µmol/min/mg enzyme

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processethanol oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-(hydroxymethyl)glutathione dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

alcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 379378Alcohol dehydrogenase class-3
PRO_0000160771

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding691Zinc 1; catalytic By similarity
Metal binding991Zinc 2 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1131Zinc 2 By similarity
Metal binding1771Zinc 1; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.11

Experimental info

Sequence conflict841E → G in AAB06322. Ref.1
Sequence conflict3541T → S in CAA57973. Ref.2

Secondary structure

............................................................................... 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 045054298F16B258

FASTA37940,699
        10         20         30         40         50         60 
MATQGQVITC KAAVAYEPNK PLVIEDVQVA PPQAGEVRIK ILYTALCHTD AYTWSGKDPE 

        70         80         90        100        110        120 
GLFPCILGHE AAGIVESVGE GVTEVQAGDH VIPCYQAECR ECKFCKSGKT NLCGKVRSAT 

       130        140        150        160        170        180 
GVGIMMNDRK SRFSVNGKPI YHFMGTSTFS QYTVVHDVSV AKIDPTAPLD KVCLLGCGVP 

       190        200        210        220        230        240 
TGLGAVWNTA KVEPGSNVAI FGLGTVGLAV AEGAKTAGAS RIIGIDIDSK KYETAKKFGV 

       250        260        270        280        290        300 
NEFVNPKDHD KPIQEVIVDL TDGGVDYSFE CIGNVSVMRA ALECCHKGWG TSVIVGVAAS 

       310        320        330        340        350        360 
GQEISTRPFQ LVTGRVWKGT AFGGFKSRTQ VPWLVEKYMN KEIKVDEYIT HNLTLGEINK 

       370 
AFDLLHEGTC LRCVLDTSK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS71244.
RefSeqNP_199207.1. NM_123761.3.
UniGeneAt.23457.
At.63885.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UKOX-ray1.40A/B2-379[»]
4GL4X-ray1.80A/B2-379[»]
4JJIX-ray1.80A/B2-379[»]
4L0QX-ray1.95A/B2-379[»]
ProteinModelPortalQ96533.
SMRQ96533. Positions 2-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19667. 2 interactions.

Proteomic databases

PaxDbQ96533.
PRIDEQ96533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G43940.1; AT5G43940.1; AT5G43940. [Q96533-1]
GeneID834417.
KEGGath:AT5G43940.

Organism-specific databases

TAIRAT5G43940.

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
InParanoidQ96533.
KOK00121.
PhylomeDBQ96533.
ProtClustDBCLSN2686871.

Enzyme and pathway databases

BioCycARA:AT5G43940-MONOMER.
ARA:GQT-1380-MONOMER.
SABIO-RKQ96533.

Gene expression databases

GenevestigatorQ96533.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR014183. 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]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
TIGRFAMsTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ96533.

Entry information

Entry nameADHX_ARATH
AccessionPrimary (citable) accession number: Q96533
Secondary accession number(s): Q0WWE1, Q43384, Q9FND2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names