ID 4CL1_PETCR Reviewed; 544 AA. AC P14912; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 02-SEP-2026, entry version 88. DE RecName: Full=4-coumarate--CoA ligase 1; DE Short=4CL 1; DE EC=6.2.1.12 {ECO:0000250|UniProtKB:O24146}; DE AltName: Full=4-coumaroyl-CoA synthase 1; GN Name=4CL1; Synonyms=4CL-1; OS Petroselinum crispum (Parsley) (Petroselinum hortense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade; OC Apieae; Petroselinum. OX NCBI_TaxID=4043; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3169018; DOI=10.1111/j.1432-1033.1988.tb14328.x; RA Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., Hahlbrock K.; RT "Primary structures and catalytic properties of isoenzymes encoded by the RT two 4-coumarate:CoA ligase genes in parsley."; RL Eur. J. Biochem. 176:661-667(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. RX PubMed=16453765; DOI=10.1002/j.1460-2075.1987.tb02353.x; RA Douglas C., Hoffmann H., Schulz W., Hahlbrock K.; RT "Structure and elicitor or U.V.-light-stimulated expression of two 4- RT coumarate:CoA ligase genes in parsley."; RL EMBO J. 6:1189-1195(1987). CC -!- FUNCTION: Carboxylate--CoA ligase that may use 4-coumarate as CC substrate. Follows a two-step reaction mechanism, wherein the CC carboxylate substrate first undergoes adenylation by ATP, followed by a CC thioesterification in the presence of CoA to yield the final CoA CC thioester. {ECO:0000250|UniProtKB:O24146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + CC diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP + CC diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:192348; Evidence={ECO:0000250|UniProtKB:O24146}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+); CC Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:O24146}; CC -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene CC biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step CC 1/2. {ECO:0000250|UniProtKB:Q42524}. CC -!- INDUCTION: By fungal elicitor and UV irradiation. CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in CC the substrate recognition, and are sufficient to confer the substrate CC specificity. {ECO:0000250|UniProtKB:Q42524}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X13324; CAA31696.1; -; mRNA. DR EMBL; X05350; CAA28959.1; -; Genomic_DNA. DR PIR; S01667; S01667. DR AlphaFoldDB; P14912; -. DR SMR; P14912; -. DR BRENDA; 6.2.1.12; 4694. DR UniPathway; UPA00372; UER00547. DR GO; GO:0106286; F:(E)-caffeate-CoA ligase activity; IEA:UniProtKB-ARBA. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; ISS:UniProtKB. DR GO; GO:0050563; F:trans-feruloyl-CoA synthase activity; IEA:UniProtKB-ARBA. DR CDD; cd05904; 4CL; 1. DR FunFam; 3.30.300.30:FF:000007; 4-coumarate--CoA ligase 2; 1. DR FunFam; 3.40.50.12780:FF:000003; Long-chain-fatty-acid--CoA ligase FadD; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR InterPro; IPR045851; AMP-b_sf. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. DR InterPro; IPR042099; ANL_N_sf. DR PANTHER; PTHR24096:SF406; 4-COUMARATE--COA LIGASE 2; 1. DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 2: Evidence at transcript level; KW ATP-binding; Ligase; Magnesium; Nucleotide-binding; KW Phenylpropanoid metabolism. FT CHAIN 1..544 FT /note="4-coumarate--CoA ligase 1" FT /id="PRO_0000193033" FT REGION 263..332 FT /note="SBD1" FT /evidence="ECO:0000250|UniProtKB:Q42524" FT REGION 333..400 FT /note="SBD2" FT /evidence="ECO:0000250|UniProtKB:Q42524" FT BINDING 190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 240 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 261 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 310 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 332 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 332 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 333 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 337 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 345 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 421 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 436 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 438 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 442 FT /ligand="(E)-4-coumaroyl-AMP" FT /ligand_id="ChEBI:CHEBI:192348" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 444 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 445 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:O24146" FT BINDING 527 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O24146" SQ SEQUENCE 544 AA; 59825 MW; 22BBAD78F255D0C8 CRC64; MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ LKASQAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVIN SDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGDNP NLYMHSEDVM ICILPLFHIY SLNAVLCCGL RAGVTILIMQ KFDIVPFLEL IQKYKVTIGP FVPPIVLAIA KSPVVDKYDL SSVRTVMSGA APLGKELEDA VRAKFPNAKL GQGYGMTEAG PVLAMCLAFA KEPYEIKSGA CGTVVRNAEM KIVDPETNAS LPRNQRGEIC IRGDQIMKGY LNDPESTRTT IDEEGWLHTG DIGFIDDDDE LFIVDRLKEI IKYKGFQVAP AELEALLLTH PTISDAAVVP MIDEKAGEVP VAFVVRTNGF TTTEEEIKQF VSKQVVFYKR IFRVFFVDAI PKSPSGKILR KDLRARIASG DLPK //