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Q96533

- ADHX_ARATH

UniProt

Q96533 - ADHX_ARATH

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
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    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

    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-SubCell

    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

    MATQGQVITC KAAVAYEPNK PLVIEDVQVA PPQAGEVRIK ILYTALCHTD    50
    AYTWSGKDPE GLFPCILGHE AAGIVESVGE GVTEVQAGDH VIPCYQAECR 100
    ECKFCKSGKT NLCGKVRSAT GVGIMMNDRK SRFSVNGKPI YHFMGTSTFS 150
    QYTVVHDVSV AKIDPTAPLD KVCLLGCGVP TGLGAVWNTA KVEPGSNVAI 200
    FGLGTVGLAV AEGAKTAGAS RIIGIDIDSK KYETAKKFGV NEFVNPKDHD 250
    KPIQEVIVDL TDGGVDYSFE CIGNVSVMRA ALECCHKGWG TSVIVGVAAS 300
    GQEISTRPFQ LVTGRVWKGT AFGGFKSRTQ VPWLVEKYMN KEIKVDEYIT 350
    HNLTLGEINK AFDLLHEGTC LRCVLDTSK 379
    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

    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 1, 2014
    This is version 128 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