P48523 · CADH4_ARATH
- ProteinCinnamyl alcohol dehydrogenase 4
- GeneCAD4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in lignin biosynthesis in the floral stem. 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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
47 μM | 4-coumaraldehyde | 6.25-6.5 | 35 | |||
87 μM | caffeyl aldehyde | 6.25 | 30 | |||
65 μM | coniferaldehyde | 6.25-6.5 | 35 | |||
85 μM | 5-hydroxyconiferaldehyde | 6.25-6.5 | 30 | |||
274 μM | sinapaldehyde | 6.25-6.5 | 30 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
44 pmol/sec/ug | 6.25-6.5 | 35 | with 4-coumaraldehyde as substrate | ||
17.1 pmol/sec/ug | 6.25 | 30 | with caffeyl aldehyde as substrate | ||
26.8 pmol/sec/ug | 6.25-6.5 | 35 | with coniferaldehyde as substrate | ||
32.3 pmol/sec/ug | 6.25-6.5 | 30 | with 5-hydroxyconiferaldehyde as substrate | ||
9.2 pmol/sec/ug | 6.25-6.5 | 30 | with sinapaldehyde as substrate |
Pathway
Aromatic compound metabolism; phenylpropanoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 50 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 70 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 71 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 101 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 107 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 115 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 168 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 189-194 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GLGGVG | ||||||
Binding site | 212-217 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SSSDKK | ||||||
Binding site | 252 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 276 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 299-301 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SFI |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 nameCinnamyl alcohol dehydrogenase 4
- EC number
- Short namesAtCAD4
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP48523
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Reduced lignin content and rigidity of the floral stems.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000160790 | 1-365 | Cinnamyl alcohol dehydrogenase 4 | |||
Sequence: MGSVEAGEKKALGWAARDPSGVLSPYSYTLRSTGADDVYIKVICCGICHTDIHQIKNDLGMSNYPMVPGHEVVGEVLEVGSDVSKFTVGDVVGVGVVVGCCGSCKPCSSELEQYCNKRIWSYNDVYTDGKPTQGGFADTMIVNQKFVVKIPEGMAVEQAAPLLCAGVTVYSPLSHFGLMASGLKGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKKEEAIEHLGADDYVVSSDPAEMQRLADSLDYIIDTVPVFHPLDPYLACLKLDGKLILMGVINTPLQFVTPLVILGRKVISGSFIGSIKETEEVLAFCKEKGLTSTIETVKIDELNIAFERLRKNDVRYRFVVDVAGSNLVEEAATTTN |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at the lateral root initiation sites, in the vascular tissues of the primary lateral root and the root caps. Expressed in the hypocotyl, cotyledon and leaf veins, apical meristem region, hydathodes, at the base of the trichomes and cauline leaves. In stems, expressed in the cells associated with the vascular cambium, interfascicular cambium and the developing xylem. Expressed in the vascular strand of petals and sepals, anthers, stamen filaments, stigma with papillary cells in flowers, and abscission, style and stigmatic regions of siliques.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)39,098
- Last updated1996-02-01 v1
- Checksum10675455727DC689
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 139 | in Ref. 3; CAP09015 | ||||
Sequence: T → A | ||||||
Sequence conflict | 234 | in Ref. 3; CAP09015 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z31715 EMBL· GenBank· DDBJ | CAA83508.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY302081 EMBL· GenBank· DDBJ | AAP59434.1 EMBL· GenBank· DDBJ | mRNA | ||
AM887553 EMBL· GenBank· DDBJ | CAP09010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887554 EMBL· GenBank· DDBJ | CAP09011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887555 EMBL· GenBank· DDBJ | CAP09012.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887556 EMBL· GenBank· DDBJ | CAP09013.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887557 EMBL· GenBank· DDBJ | CAP09014.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887558 EMBL· GenBank· DDBJ | CAP09015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887559 EMBL· GenBank· DDBJ | CAP09016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887560 EMBL· GenBank· DDBJ | CAP09017.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887561 EMBL· GenBank· DDBJ | CAP09018.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887562 EMBL· GenBank· DDBJ | CAP09019.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887563 EMBL· GenBank· DDBJ | CAP09020.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887564 EMBL· GenBank· DDBJ | CAP09021.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887565 EMBL· GenBank· DDBJ | CAP09022.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887566 EMBL· GenBank· DDBJ | CAP09023.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887567 EMBL· GenBank· DDBJ | CAP09024.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887568 EMBL· GenBank· DDBJ | CAP09025.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887569 EMBL· GenBank· DDBJ | CAP09026.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887570 EMBL· GenBank· DDBJ | CAP09027.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887571 EMBL· GenBank· DDBJ | CAP09028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM887572 EMBL· GenBank· DDBJ | CAP09029.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB025624 EMBL· GenBank· DDBJ | BAB02470.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE76241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370261 EMBL· GenBank· DDBJ | AAK44076.1 EMBL· GenBank· DDBJ | mRNA | ||
AY042841 EMBL· GenBank· DDBJ | AAK68781.1 EMBL· GenBank· DDBJ | mRNA | ||
AY063076 EMBL· GenBank· DDBJ | AAL34250.1 EMBL· GenBank· DDBJ | mRNA | ||
AY088220 EMBL· GenBank· DDBJ | AAM65761.1 EMBL· GenBank· DDBJ | mRNA |