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Q96533

- ADHX_ARATH

UniProt

Q96533 - ADHX_ARATH

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Protein

Alcohol dehydrogenase class-3

Gene

ADH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Binds 2 zinc ions per subunit.By similarity

Kineticsi

  1. KM=1.4 µM for S-(hydroxymethyl)glutathione

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

  1. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
  2. S-(hydroxymethyl)glutathione dehydrogenase activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. ethanol oxidation Source: InterPro
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_187605. Abacavir metabolism.
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: Chromosome 5

Organism-specific databases

TAIRiAT5G43940.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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

Gene expression databases

GenevestigatoriQ96533.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi19667. 2 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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. Align

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S71244.
RefSeqi NP_199207.1. NM_123761.3. [Q96533-1 ]
UniGenei At.23457.
At.63885.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UKO X-ray 1.40 A/B 2-379 [» ]
4GL4 X-ray 1.80 A/B 2-379 [» ]
4JJI X-ray 1.80 A/B 2-379 [» ]
4L0Q X-ray 1.95 A/B 2-379 [» ]
ProteinModelPortali Q96533.
SMRi Q96533. Positions 2-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 19667. 2 interactions.

Proteomic databases

PaxDbi Q96533.
PRIDEi Q96533.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G43940.1 ; AT5G43940.1 ; AT5G43940 . [Q96533-1 ]
GeneIDi 834417.
KEGGi ath:AT5G43940.

Organism-specific databases

TAIRi AT5G43940.

Phylogenomic databases

eggNOGi COG1062.
HOGENOMi HOG000294674.
InParanoidi Q96533.
KOi K00121.
PhylomeDBi Q96533.

Enzyme and pathway databases

BioCyci ARA:AT5G43940-MONOMER.
ARA:GQT-1380-MONOMER.
Reactomei REACT_187605. Abacavir metabolism.
SABIO-RK Q96533.

Miscellaneous databases

PROi Q96533.

Gene expression databases

Genevestigatori Q96533.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR014183. 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 ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 2 hits.
TIGRFAMsi TIGR02818. adh_III_F_hyde. 1 hit.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 129 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