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Q02972 (CADH8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cinnamyl alcohol dehydrogenase 8

Short name=AtCAD8
EC=1.1.1.195
Alternative name(s):
NAD-dependent mannitol dehydrogenase 2
Gene names
Name:CAD8
Synonyms:BAD, CAD5, CADB2, ELI3-2
Ordered Locus Names:At4g37990
ORF Names:F20D10.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

Cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Aromatic compound metabolism; phenylpropanoid biosynthesis.

Subunit structure

Homodimer By similarity.

Tissue specificity

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. Ref.6 Ref.7

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=302 µM for 4-coumaraldehyde (at pH 6.25 and 42 degrees Celsius) Ref.2

KM=683 µM for caffeyl aldehyde (at pH 6.0 and 35 degrees Celsius)

KM=141 µM for coniferaldehyde (at pH 6.25 and 42 degrees Celsius)

KM=457 µM for 5-hydroxyconiferaldehyde (at pH 6.25 and 42 degrees Celsius)

KM=898 µM for sinapaldehyde (at pH 6.25-6.5 and 25 degrees Celsius)

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

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

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Cinnamyl alcohol dehydrogenase 8
PRO_0000160809

Regions

Nucleotide binding187 – 1926NADP By similarity
Nucleotide binding210 – 2156NADP By similarity
Nucleotide binding297 – 2993NADP By similarity

Sites

Metal binding461Zinc 1; catalytic By similarity
Metal binding681Zinc 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 binding1621Zinc 1; catalytic By similarity
Binding site481NADP By similarity
Binding site1661NADP By similarity
Binding site2501NADP By similarity
Binding site2741NADP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02972 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B691F9B8AD4842A5

FASTA35938,942
        10         20         30         40         50         60 
MGKVLQKEAF GLAAKDNSGV LSPFSFTRRE TGEKDVRFKV LFCGICHSDL HMVKNEWGMS 

        70         80         90        100        110        120 
TYPLVPGHEI VGVVTEVGAK VTKFKTGEKV GVGCLVSSCG SCDSCTEGME NYCPKSIQTY 

       130        140        150        160        170        180 
GFPYYDNTIT YGGYSDHMVC EEGFVIRIPD NLPLDAAAPL LCAGITVYSP MKYHGLDKPG 

       190        200        210        220        230        240 
MHIGVVGLGG LGHVGVKFAK AMGTKVTVIS TSEKKRDEAI NRLGADAFLV SRDPKQIKDA 

       250        260        270        280        290        300 
MGTMDGIIDT VSATHSLLPL LGLLKHKGKL VMVGAPEKPL ELPVMPLIFE RKMVMGSMIG 

       310        320        330        340        350 
GIKETQEMID MAGKHNITAD IELISADYVN TAMERLEKAD VRYRFVIDVA NTLKPNPNL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS28043.
RefSeqNP_195512.1. NM_119960.2.
UniGeneAt.41.

3D structure databases

ProteinModelPortalQ02972.
SMRQ02972. Positions 8-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G37990.1-P.

Proteomic databases

PaxDbQ02972.
PRIDEQ02972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G37990.1; AT4G37990.1; AT4G37990.
GeneID829955.
KEGGath:AT4G37990.

Organism-specific databases

TAIRAT4G37990.

Phylogenomic databases

eggNOGCOG1064.
HOGENOMHOG000294667.
InParanoidQ02972.
KOK00083.
OMAKLDWNLY.
PhylomeDBQ02972.

Enzyme and pathway databases

BioCycARA:AT4G37990-MONOMER.
SABIO-RKQ02972.
UniPathwayUPA00711.

Gene expression databases

GenevestigatorQ02972.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. 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. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCADH8_ARATH
AccessionPrimary (citable) accession number: Q02972
Secondary accession number(s): Q53ZN2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 108 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names