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Protein

Cinnamyl alcohol dehydrogenase 8

Gene

CAD8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Zn2+By similarityNote: Binds 2 Zn2+ 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
Complete GO annotation...

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.
OMAiRLGDCPE.
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

        10         20         30         40         50
MGKVLQKEAF GLAAKDNSGV LSPFSFTRRE TGEKDVRFKV LFCGICHSDL
60 70 80 90 100
HMVKNEWGMS TYPLVPGHEI VGVVTEVGAK VTKFKTGEKV GVGCLVSSCG
110 120 130 140 150
SCDSCTEGME NYCPKSIQTY GFPYYDNTIT YGGYSDHMVC EEGFVIRIPD
160 170 180 190 200
NLPLDAAAPL LCAGITVYSP MKYHGLDKPG MHIGVVGLGG LGHVGVKFAK
210 220 230 240 250
AMGTKVTVIS TSEKKRDEAI NRLGADAFLV SRDPKQIKDA MGTMDGIIDT
260 270 280 290 300
VSATHSLLPL LGLLKHKGKL VMVGAPEKPL ELPVMPLIFE RKMVMGSMIG
310 320 330 340 350
GIKETQEMID MAGKHNITAD IELISADYVN TAMERLEKAD VRYRFVIDVA

NTLKPNPNL
Length:359
Mass (Da):38,942
Last modified:November 1, 1995 - v1
Checksum:iB691F9B8AD4842A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi3702.AT4G37990.1-P.

Proteomic databases

PaxDbiQ02972.
PRIDEiQ02972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G37990.

Phylogenomic databases

eggNOGiCOG1064.
HOGENOMiHOG000294667.
InParanoidiQ02972.
KOiK00083.
OMAiRLGDCPE.
PhylomeDBiQ02972.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatoriQ02972.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 111 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

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.