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Q02972

- CADH8_ARATH

UniProt

Q02972 - CADH8_ARATH

Protein

Cinnamyl alcohol dehydrogenase 8

Gene

CAD8

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 109 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.1 Publication

    Catalytic activityi

    Cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Kineticsi

    1. KM=302 µM for 4-coumaraldehyde (at pH 6.25 and 42 degrees Celsius)1 Publication
    2. KM=683 µM for caffeyl aldehyde (at pH 6.0 and 35 degrees Celsius)1 Publication
    3. KM=141 µM for coniferaldehyde (at pH 6.25 and 42 degrees Celsius)1 Publication
    4. KM=457 µM for 5-hydroxyconiferaldehyde (at pH 6.25 and 42 degrees Celsius)1 Publication
    5. KM=898 µM for sinapaldehyde (at pH 6.25-6.5 and 25 degrees Celsius)1 Publication

    Vmax=20.4 pmol/sec/µg enzyme with 4-coumaraldehyde as substrate (at pH 6.25 and 42 degrees Celsius)1 Publication

    Vmax=7.0 pmol/sec/µg enzyme with caffeyl aldehyde as substrate (at pH 6.0 and 35 degrees Celsius)1 Publication

    Vmax=5.6 pmol/sec/µg enzyme with coniferaldehyde as substrate (at pH 6.25 and 42 degrees Celsius)1 Publication

    Vmax=10.4 pmol/sec/µg enzyme with 5-hydroxyconiferaldehyde as substrate (at pH 6.25 and 42 degrees Celsius)1 Publication

    Vmax=28.9 pmol/sec/µg enzyme with sinapaldehyde as substrate (at pH 6.25-6.5 and 25 degrees Celsius)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi46 – 461Zinc 1; catalyticBy similarity
    Binding sitei48 – 481NADPBy similarity
    Metal bindingi68 – 681Zinc 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 bindingi162 – 1621Zinc 1; catalyticBy similarity
    Binding sitei166 – 1661NADPBy similarity
    Binding sitei250 – 2501NADPBy similarity
    Binding sitei274 – 2741NADP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPBy similarity
    Nucleotide bindingi210 – 2156NADPBy similarity
    Nucleotide bindingi297 – 2993NADPBy similarity

    GO - Molecular functioni

    1. aryl-alcohol dehydrogenase (NADP+) activity Source: TAIR
    2. cinnamyl-alcohol dehydrogenase activity Source: UniProtKB
    3. sinapyl alcohol dehydrogenase activity Source: UniProtKB-EC
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. lignin biosynthetic process Source: UniProtKB
    2. response to bacterium Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin biosynthesis

    Keywords - Ligandi

    Metal-binding, NADP, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT4G37990-MONOMER.
    SABIO-RKQ02972.
    UniPathwayiUPA00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cinnamyl alcohol dehydrogenase 8 (EC:1.1.1.195)
    Short name:
    AtCAD8
    Alternative name(s):
    NAD-dependent mannitol dehydrogenase 2
    Gene namesi
    Name:CAD8
    Synonyms:BAD, CAD5, CADB2, ELI3-2
    Ordered Locus Names:At4g37990
    ORF Names:F20D10.110
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G37990.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Cinnamyl alcohol dehydrogenase 8PRO_0000160809Add
    BLAST

    Proteomic databases

    PaxDbiQ02972.
    PRIDEiQ02972.

    Expressioni

    Tissue specificityi

    Expressed in the differentiation and elongation zones of primary and lateral roots. Expressed in the hypocotyl, cotyledon veins, vasculature of the first rosette leaves, hydathodes and trichomes. In stems, expressed in the vascular cambium and developing xylem tissues. Expressed in the style, anthers, stamen filaments, stigmatic regions in flowers, and abscission and style regions of siliques.2 Publications

    Gene expression databases

    GenevestigatoriQ02972.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT4G37990.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02972.
    SMRiQ02972. Positions 8-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1064.
    HOGENOMiHOG000294667.
    InParanoidiQ02972.
    KOiK00083.
    OMAiKLDWNLY.
    PhylomeDBiQ02972.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. 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. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02972-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKVLQKEAF GLAAKDNSGV LSPFSFTRRE TGEKDVRFKV LFCGICHSDL    50
    HMVKNEWGMS TYPLVPGHEI VGVVTEVGAK VTKFKTGEKV GVGCLVSSCG 100
    SCDSCTEGME NYCPKSIQTY GFPYYDNTIT YGGYSDHMVC EEGFVIRIPD 150
    NLPLDAAAPL LCAGITVYSP MKYHGLDKPG MHIGVVGLGG LGHVGVKFAK 200
    AMGTKVTVIS TSEKKRDEAI NRLGADAFLV SRDPKQIKDA MGTMDGIIDT 250
    VSATHSLLPL LGLLKHKGKL VMVGAPEKPL ELPVMPLIFE RKMVMGSMIG 300
    GIKETQEMID MAGKHNITAD IELISADYVN TAMERLEKAD VRYRFVIDVA 350
    NTLKPNPNL 359
    Length:359
    Mass (Da):38,942
    Last modified:November 1, 1995 - v1
    Checksum:iB691F9B8AD4842A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67815 mRNA. Translation: CAA48026.1.
    AY302080 mRNA. Translation: AAP59433.1.
    AL035538 Genomic DNA. Translation: CAB37539.1.
    AL161592 Genomic DNA. Translation: CAB80464.1.
    CP002687 Genomic DNA. Translation: AEE86861.1.
    AF361859 mRNA. Translation: AAK32871.1.
    AY129478 mRNA. Translation: AAM91064.1.
    PIRiS28043.
    RefSeqiNP_195512.1. NM_119960.2.
    UniGeneiAt.41.

    Genome annotation databases

    EnsemblPlantsiAT4G37990.1; AT4G37990.1; AT4G37990.
    GeneIDi829955.
    KEGGiath:AT4G37990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67815 mRNA. Translation: CAA48026.1 .
    AY302080 mRNA. Translation: AAP59433.1 .
    AL035538 Genomic DNA. Translation: CAB37539.1 .
    AL161592 Genomic DNA. Translation: CAB80464.1 .
    CP002687 Genomic DNA. Translation: AEE86861.1 .
    AF361859 mRNA. Translation: AAK32871.1 .
    AY129478 mRNA. Translation: AAM91064.1 .
    PIRi S28043.
    RefSeqi NP_195512.1. NM_119960.2.
    UniGenei At.41.

    3D structure databases

    ProteinModelPortali Q02972.
    SMRi Q02972. Positions 8-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G37990.1-P.

    Proteomic databases

    PaxDbi Q02972.
    PRIDEi Q02972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G37990.1 ; AT4G37990.1 ; AT4G37990 .
    GeneIDi 829955.
    KEGGi ath:AT4G37990.

    Organism-specific databases

    TAIRi AT4G37990.

    Phylogenomic databases

    eggNOGi COG1064.
    HOGENOMi HOG000294667.
    InParanoidi Q02972.
    KOi K00083.
    OMAi KLDWNLY.
    PhylomeDBi Q02972.

    Enzyme and pathway databases

    UniPathwayi UPA00711 .
    BioCyci ARA:AT4G37990-MONOMER.
    SABIO-RK Q02972.

    Gene expression databases

    Genevestigatori Q02972.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi 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. 1 hit.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rapid activation of a novel plant defense gene is strictly dependent on the Arabidopsis RPM1 disease resistance locus."
      Kiedrowski S., Kawalleck P., Hahlbrock K., Somssich I.E., Dangl J.L.
      EMBO J. 11:4677-4684(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis."
      Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L., Davin L.B., Kang C., Lewis N.G.
      Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [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. "Evidence for a role of AtCAD 1 in lignification of elongating stems of Arabidopsis thaliana."
      Eudes A., Pollet B., Sibout R., Do C.-T., Seguin A., Lapierre C., Jouanin L.
      Planta 225:23-39(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Expression of cinnamyl alcohol dehydrogenases and their putative homologues during Arabidopsis thaliana growth and development: lessons for database annotations?"
      Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.
      Phytochemistry 68:1957-1974(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCADH8_ARATH
    AccessioniPrimary (citable) accession number: Q02972
    Secondary accession number(s): Q53ZN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3