UniProt:Q6ETN3 4CL3

chain
  • chain:1-554
checksum 5A1A9D84734BB13C
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: ferulate > 4-coumarate > caffeate > cinnamate (PubMed:21807887). Possesses very high activity compared to 4CL1, 4CL2, 4CL4 and 4CL5 (PubMed:21807887). Cannot convert sinapate to its corresponding CoA ester (PubMed:21807887, PubMed:23246835). May play a role in the synthesis of lignin as well as other phenolic compounds (PubMed:21807887). 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 (By similarity).CATALYTIC ACTIVITY (E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-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)-ferulate + ATP + H(+) = (E)-feruloyl-AMP + diphosphateCATALYTIC ACTIVITY (E)-feruloyl-AMP + CoA = (E)-feruloyl-CoA + AMP + H(+)CATALYTIC 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(+)COFACTOR kcat is 10.92 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 17.1 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 15.3 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 17.94 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.TISSUE SPECIFICITY Expressed in root exodermis and epidermis cells, stem vascular cells, leaf developing vascular bundle cells and parenchyma cells, lemma, palea, stamens and pistil.INDUCTION Induced by wounding (PubMed:23246835). Down-regulated by UV irradiation (PubMed:23246835).DOMAIN Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.MISCELLANEOUS Plants silencing 4CL3 exhibit significant lignin reduction, reduced plant height, decreased panicle fertility and abnormal anther development.SIMILARITY Belongs to the ATP-dependent AMP-binding enzyme family.
created [InstanceEdit:1164949] Wu, Guanming, 2010-12-11
crossReference
databaseName UniProt
dbId 1162142
description
  • recommendedName: fullName evidence="5"4-coumarate--CoA ligase 3 shortName evidence="5"4CL 3 shortName evidence="5"Os4CL3 ecNumber evidence="3 4"6.2.1.12 alternativeName: fullName evidence="6"(E)-ferulate--CoA ligase ecNumber evidence="3 4"6.2.1.34 alternativeName: fullName evidence="6"4-coumaroyl-CoA synthase 3
displayName UniProt:Q6ETN3 4CL3
geneName
  • 4CL3
  • Os02g0177600
  • LOC_Os02g08100
  • OsJ_005431
  • P0504A05.24
identifier Q6ETN3
isSequenceChanged false
keyword
  • ATP-binding
  • Ligase
  • Magnesium
  • Nucleotide-binding
  • Phenylpropanoid metabolism
  • Reference proteome
modified [InstanceEdit:9852000] Weiser, Joel, 2023-11-03
name
  • 4CL3
referenceDatabase [ReferenceDatabase:2] UniProt
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • 4CL3_ORYSJ
sequenceLength 554
species [Species:1250427] Oryza sativa subsp. japonica
url http://purl.uniprot.org/uniprot/Q6ETN3