UniProt:P17814 4CL1

chain
  • chain:1-564
checksum 9725A4B4A72F8C6E
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 > cinnamate > caffeate (PubMed:21807887). Cannot convert sinapate to its corresponding CoA ester (PubMed:21807887, PubMed:23246835). 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)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphateCATALYTIC ACTIVITY (E)-caffeate + ATP + CoA = (E)-caffeoyl-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 0.37 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 0.49 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.52 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 0.41 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 roots, stems, leaf blades and leaf sheaths.INDUCTION Induced by fungal elicitor and UV irradiation. Down-regulated by wounding and 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.SIMILARITY Belongs to the ATP-dependent AMP-binding enzyme family.SEQUENCE CAUTION Truncated N-terminus.
created [InstanceEdit:1164949] Wu, Guanming, 2010-12-11
crossReference
databaseName UniProt
dbId 1161745
description
  • recommendedName: fullName evidence="5"4-coumarate--CoA ligase 1 shortName evidence="5"4CL 1 shortName evidence="5"Os4CL1 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 1
displayName UniProt:P17814 4CL1
geneName
  • 4CL1
  • 4CL
  • Os08g0245200
  • LOC_Os08g14760
  • OJ1033_B09.16
identifier P17814
isSequenceChanged false
keyword
  • ATP-binding
  • Ligase
  • Magnesium
  • Nucleotide-binding
  • Phenylpropanoid metabolism
  • Reference proteome
modified [InstanceEdit:9852000] Weiser, Joel, 2023-11-03
name
  • 4CL1
referenceDatabase [ReferenceDatabase:2] UniProt
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • 4CL1_ORYSJ
  • B7EH38
  • Q0J6Z8
  • Q6ZKV9
sequenceLength 564
species [Species:1250427] Oryza sativa subsp. japonica
url http://purl.uniprot.org/uniprot/P17814