Q67W82 · 4CL4_ORYSJ
- Protein4-coumarate--CoA ligase 4
- Gene4CL4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites (PubMed:21807887, PubMed:23246835).
Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate (PubMed:21807887, PubMed:23246835).
Is more efficient with substrates in the following order: 4-coumarate > ferulate > caffeate > cinnamate (PubMed:21807887).
Cannot convert sinapate to its corresponding CoA ester (PubMed:21807887, PubMed:23246835).
Required for the biosynthesis of lignin in roots and shoots (PubMed:32989851).
Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioesters (By similarity).
Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate (PubMed:21807887, PubMed:23246835).
Is more efficient with substrates in the following order: 4-coumarate > ferulate > caffeate > cinnamate (PubMed:21807887).
Cannot convert sinapate to its corresponding CoA ester (PubMed:21807887, PubMed:23246835).
Required for the biosynthesis of lignin in roots and shoots (PubMed:32989851).
Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioesters (By similarity).
Catalytic activity
- (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-4-coumarate + ATP + H+ = (E)-4-coumaroyl-AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H+This reaction proceeds in the forward direction.
- (E)-caffeate + ATP + H+ = (E)-caffeoyl-AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-caffeoyl-AMP + CoA = (E)-caffeoyl-CoA + AMP + H+This reaction proceeds in the forward direction.
- (E)-ferulate + ATP + H+ = (E)-feruloyl-AMP + diphosphateThis reaction proceeds in the forward direction.
- (E)-feruloyl-AMP + CoA = (E)-feruloyl-CoA + AMP + H+This reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
15.7 μM | cinnamate | |||||
3.9 μM | 4-coumarate | |||||
5.8 μM | caffeate | |||||
4.6 μM | ferulate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
350 pmol/sec/mg | with cinnamate as substrate | ||||
770 pmol/sec/mg | with 4-coumarate as substrate | ||||
590 pmol/sec/mg | with caffeate as substrate | ||||
520 pmol/sec/mg | with ferulate as substrate |
kcat is 1.28 min-1 with cinnamate as substrate (PubMed:21807887).
kcat is 2.82 min-1 with 4-coumarate as substrate (PubMed:21807887).
kcat is 2.16 min-1 with caffeate as substrate (PubMed:21807887).
kcat is 1.92 min-1 with ferulate as substrate (PubMed:21807887).
kcat is 2.82 min-1 with 4-coumarate as substrate (PubMed:21807887).
kcat is 2.16 min-1 with caffeate as substrate (PubMed:21807887).
kcat is 1.92 min-1 with ferulate as substrate (PubMed:21807887).
Pathway
Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 198 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 199 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 200 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 201 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 202 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 206 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 248 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 252 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 269 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 318 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 340 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 340 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 341 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 341 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 345 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 345 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 353 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 429 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 444 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 446 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 450 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 452 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 453 | CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 535 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | (E)-caffeate-CoA ligase activity | |
Molecular Function | 4-coumarate-CoA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | CoA-ligase activity | |
Molecular Function | trans-cinnamate-CoA ligase activity | |
Biological Process | lignin biosynthetic process | |
Biological Process | phenylpropanoid metabolic process | |
Biological Process | response to aluminum ion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-coumarate--CoA ligase 4
- EC number
- Short names4CL 4 ; Os4CL4
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ67W82
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 395 | In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum. | ||||
Sequence: G → R |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000351625 | 1-559 | 4-coumarate--CoA ligase 4 | |||
Sequence: MGSMAAAAEAAQEEETVVFRSKLPDIEIPSHLTLQAYCFEKLPEVAARPCLIDGQTGAVYSYGEVEELSRRAAAGLRRLGVGKGDVVMSLLRNCPEFAFTFLGAARLGAATTTANPFYTPHEIHRQASAAGARVIVTEACAVEKVRGFAADRGIPVVAVDGDFDGCVGFGEAMLDASIEPLDADEEVHPDDVVALPYSSGTTGLPKGVMLTHRSLVTSVAQQVDGENPNLYFRREDVVLCLLPLFHIYSLNSVLLAGLRAGSAIVIMRKFDLGALVDLTRRHGVTVAPFVPPIVVEIAKSPRVTADDLASIRMVMSGAAPMGKDLQDAFMAKIPNAVLGQGYGMTEAGPVLAMCLAFAKEPFEVKSGSCGTVVRNAELKIVDPDTGATLGRNQSGEICIRGEQIMKGYLNDPESTKNTIDKGGWLHTGDIGYVDDDDEIFIVDRLKEIIKYKGFQVPPAELEALLITHPDIKDAAVVPMIDEIAGEVPVAFIVRIEGSAISENEIKQFVAKEVVFYKRLNKVFFADSIPKSPSGKILRKDLRAKLAAGIPTNDNTQLKS |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 271-340 | SBD1 | ||||
Sequence: DLGALVDLTRRHGVTVAPFVPPIVVEIAKSPRVTADDLASIRMVMSGAAPMGKDLQDAFMAKIPNAVLGQ | ||||||
Region | 341-408 | SBD2 | ||||
Sequence: GYGMTEAGPVLAMCLAFAKEPFEVKSGSCGTVVRNAELKIVDPDTGATLGRNQSGEICIRGEQIMKGY |
Domain
Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q67W82-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length559
- Mass (Da)60,029
- Last updated2004-10-11 v1
- ChecksumDAC957A75C3E45BA
Q67W82-2
- Name2
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP003712 EMBL· GenBank· DDBJ | BAD37587.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP003712 EMBL· GenBank· DDBJ | BAD37588.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008212 EMBL· GenBank· DDBJ | BAF20166.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014962 EMBL· GenBank· DDBJ | BAS98942.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014962 EMBL· GenBank· DDBJ | BAS98944.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK067261 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK068985 EMBL· GenBank· DDBJ | BAG91197.1 EMBL· GenBank· DDBJ | mRNA |