P50746 · CADH_EUCBO
- ProteinProbable cinnamyl alcohol dehydrogenase
- GeneCAD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- (E)-cinnamyl alcohol + NADP+ = (E)-cinnamaldehyde + H+ + NADPHThis reaction proceeds in the backward direction.
- (E)-caffeyl alcohol + NADP+ = (E)-caffeyl aldehyde + H+ + NADPHThis reaction proceeds in the backward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Aromatic compound metabolism; phenylpropanoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 49 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 69 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 70 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 103 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 106 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 114 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 162 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 166 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 187-192 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GLGGVG | ||||||
Binding site | 210-215 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SSSDKK | ||||||
Binding site | 250 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 274 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 297-299 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SFI |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | cinnamyl-alcohol dehydrogenase activity | |
Molecular Function | coniferyl-alcohol dehydrogenase activity | |
Molecular Function | zinc ion binding | |
Biological Process | lignin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable cinnamyl alcohol dehydrogenase
- EC number
- Short namesCAD
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Myrtales > Myrtaceae > Myrtoideae > Eucalypteae > Eucalyptus
Accessions
- Primary accessionP50746
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000160792 | 1-355 | Probable cinnamyl alcohol dehydrogenase | |||
Sequence: MGSLEKERTTTGWAARDPSGVLSPYTYSLRNTGPEDLYIKVLSCGICHSDIHQIKNDLGMSHYPMVPGHEVVGEVLEVGSEVTKYRVGDRVGTGIVVGCCRSCGPCNSDQEQYCNKKIWNYNDVYTDGKPTQGGFAGEIVVGQRFVVKIPDGLESEQDAVMCAGVTVYSPLVRFGLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKRTEALEHLGADAYLVSSDENGMKEATDSLDYIFDTIPVVHPLEPYLALLKLDGKLILTGVINAPLQFISPMVMLGRKSITGSFIGSMKETEEMLEFCKEKGLTSQIEVIKMDYVNTALERLEKNDVRYRFVVDVAGSKLD |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)38,679
- Last updated1996-10-01 v1
- Checksum8F1D067A409D629A