UniProt:Q67W82 4CL4

chain
  • chain:1-559
checksum DAC957A75C3E45BA
comment
  • 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).CATALYTIC ACTIVITY (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP + diphosphateCATALYTIC ACTIVITY (E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+)CATALYTIC ACTIVITY (E)-caffeate + ATP + H(+) = (E)-caffeoyl-AMP + diphosphateCATALYTIC ACTIVITY (E)-caffeoyl-AMP + CoA = (E)-caffeoyl-CoA + AMP + H(+)CATALYTIC ACTIVITY (E)-ferulate + ATP + H(+) = (E)-feruloyl-AMP + diphosphateCATALYTIC ACTIVITY (E)-feruloyl-AMP + CoA = (E)-feruloyl-CoA + AMP + H(+)COFACTOR 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).PATHWAY Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2.SUBCELLULAR LOCATION Expressed in roots, stems, leaf blades and leaf sheaths.INDUCTION Induced by heat stress (PubMed:23994682). Induced by wounding (PubMed:23246835). Down-regulated by UV irradiation (PubMed:23246835, PubMed:23994682). Down-regulated by aluminum stress (PubMed:32989851).DOMAIN Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.SIMILARITY Belongs to the ATP-dependent AMP-binding enzyme family.
created [InstanceEdit:1164949] Wu, Guanming, 2010-12-11
crossReference
databaseName UniProt
dbId 1160525
description
  • recommendedName: fullName evidence="8"4-coumarate--CoA ligase 4 shortName evidence="8"4CL 4 shortName evidence="8"Os4CL4 ecNumber evidence="3 4"6.2.1.12 alternativeName: fullName evidence="10"(E)-ferulate--CoA ligase ecNumber evidence="3 4"6.2.1.34 alternativeName: fullName evidence="10"4-coumaroyl-CoA synthase 4 alternativeName: fullName evidence="9"Protein RESISTANCE TO ALUMINUM 1
displayName UniProt:Q67W82 4CL4
geneName
  • 4CL4
  • RAL1
  • Os06g0656500
  • LOC_Os06g44620
  • P0460H04.31-1
  • P0460H04.31-2
identifier Q67W82
isSequenceChanged false
keyword
  • Alternative splicing
  • ATP-binding
  • Cytoplasm
  • Ligase
  • Magnesium
  • Nucleotide-binding
  • Phenylpropanoid metabolism
  • Reference proteome
modified [InstanceEdit:9852000] Weiser, Joel, 2023-11-03
name
  • 4CL4
referenceDatabase [ReferenceDatabase:2] UniProt
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • 4CL4_ORYSJ
  • B7EFQ0
  • Q67W81
sequenceLength 559
species [Species:1250427] Oryza sativa subsp. japonica
url http://purl.uniprot.org/uniprot/Q67W82