Q9LQ12 · 4CLL1_ARATH
- Protein4-coumarate--CoA ligase-like 1
- Gene4CLL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids542 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Carboxylate--CoA ligase that may use 4-coumarate as substrate. 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 thioester.
Catalytic activity
- (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-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.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 189 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 190 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 191 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 192 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 193 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 197 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 237 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 258 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 309 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 331 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 331 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 332 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 332 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 336 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 336 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 420 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 435 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 437 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 441 | (E)-4-coumaroyl-AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 443 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 444 | CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 526 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Molecular Function | ATP binding | |
Molecular Function | long-chain fatty acid-CoA ligase activity | |
Molecular Function | medium-chain fatty acid-CoA ligase activity | |
Biological Process | fatty-acyl-CoA biosynthetic process | |
Biological Process | pollen development | |
Biological Process | sporopollenin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-coumarate--CoA ligase-like 1
- EC number
- 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 accessionQ9LQ12
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000299174 | 1-542 | 4-coumarate--CoA ligase-like 1 | |||
Sequence: MESQKQEDNEYIFRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKILSINKK |
Proteomic databases
Expression
Interaction
Subunit
Interacts with TKPR1, PKSA and PKSB.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9LQ12 | PKSA O23674 | 3 | EBI-30859465, EBI-30859485 | |
BINARY | Q9LQ12 | PKSB Q8LDM2 | 4 | EBI-30859465, EBI-30859537 | |
BINARY | Q9LQ12 | TKPR1 Q500U8 | 3 | EBI-30859465, EBI-4432350 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 260-331 | SBD1 | ||||
Sequence: DLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQE | ||||||
Region | 332-399 | SBD2 | ||||
Sequence: AYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGY |
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
- Sequence statusComplete
- Length542
- Mass (Da)59,169
- Last updated2000-10-01 v1
- Checksum8F055B6A1E0DF85B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY250836 EMBL· GenBank· DDBJ | AAP03019.1 EMBL· GenBank· DDBJ | mRNA | ||
AY376734 EMBL· GenBank· DDBJ | AAQ86593.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011000 EMBL· GenBank· DDBJ | AAF75805.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE34025.1 EMBL· GenBank· DDBJ | Genomic DNA |