ID   4CL_VANPL               Reviewed;         553 AA.
AC   O24540;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=4-coumarate--CoA ligase;
DE            Short=4CL;
DE            EC=6.2.1.12 {ECO:0000250|UniProtKB:Q42524};
DE   AltName: Full=4-coumaroyl-CoA synthase;
GN   Name=4CL;
OS   Vanilla planifolia (Vanilla).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Vanilloideae; Vanilleae; Vanilla.
OX   NCBI_TaxID=51239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Brodelius P., Xue Z.T.;
RT   "Isolation and characterization of a cDNA from cell suspension cultures of
RT   Vanilla planifolia encoding 4-coumarate: coenzyme A ligase.";
RL   Plant Physiol. Biochem. 35:497-506(1997).
CC   -!- FUNCTION: Produces CoA thioesters of a variety of hydroxy- and methoxy-
CC       substituted cinnamic acids, which are used to synthesize several
CC       phenylpropanoid-derived compounds, including anthocyanins, flavonoids,
CC       isoflavonoids, coumarins, lignin, suberin and wall-bound phenolics.
CC       {ECO:0000250|UniProtKB:Q42524}.
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:Q42524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC         Evidence={ECO:0000250|UniProtKB:Q42524};
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   -!- 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   AlphaFoldDB; O24540; -.
DR   SMR; O24540; -.
DR   PRIDE; O24540; -.
DR   UniPathway; UPA00372; UER00547.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism.
FT   CHAIN           1..553
FT                   /note="4-coumarate--CoA ligase"
FT                   /id="PRO_0000193042"
FT   REGION          271..340
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          341..408
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         198..202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         318..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         340..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         429
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
SQ   SEQUENCE   553 AA;  60096 MW;  9A2D250BC84EA1CB CRC64;
     MAAAVAIEEQ KKDIIFRSKL PDIYIPKNLP LHSYCFENIS KFSSRPCLIN GATDEIFTYA
     DVELISRRVG SGLSKLGIKQ GDTIMILLPN SPEFVFAFLG ASFIGSISTM ANPFFTSTEV
     IKQAKASNAK LIITQGCYVD KVKDYACENG VKIISIDTTT TADDAANILH FSELTGADEN
     EMPKVEISPD GVVALPYSSG TTGLPKGVML THKGLVTSVA QQVDGENPNL YMHSDDVLLC
     VLPLFHIYSL NSVLLCGLRA GSGILIMQKF EIVPFLELIQ KYKVTIGPFV PPIVLAIAKS
     TVVDNYDLSS VRTVMSGAAP LGKELEDAVR AKFPNAKLGQ GYGMTEAGPV LAMCLAFAKE
     PFDIKSGACG TVVRNAEMKI VDPETGSSLP RNHPGEICIR GDQIMKGYLN DPEATARTID
     KEGWLHTGDI GYIDDDDELF IVDRLKELIK YKGFQVAPAE LEALLLTHPC ISDAAVVPMK
     DEAAGEVPVA FVVKSNGHNI TEDEIKQFIS KQVIFYKRIN RVFFVEAIPK APSGKILRKD
     LRARLAAAAL PTN