4CL1_NARPS
ID 4CL1_NARPS Reviewed; 547 AA.
AC A0A2H5AIX5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=4-coumarate-CoA ligase 1 {ECO:0000303|PubMed:29229969};
DE EC=6.2.1.12 {ECO:0000250|UniProtKB:Q42524};
GN Name=4CL1 {ECO:0000303|PubMed:29229969};
OS Narcissus pseudonarcissus (Daffodil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=39639;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. King Alfred; TISSUE=Bulb;
RX PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA Singh A., Desgagne-Penix I.;
RT "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL Sci. Rep. 7:17356-17356(2017).
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 -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, to a lower extent,
CC in bulbs. {ECO:0000269|PubMed:29229969}.
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}.
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DR EMBL; MF416093; AUG71938.1; -; mRNA.
DR AlphaFoldDB; A0A2H5AIX5; -.
DR SMR; A0A2H5AIX5; -.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism.
FT CHAIN 1..547
FT /note="4-coumarate-CoA ligase 1"
FT /id="PRO_0000450635"
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..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 310..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 332..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
SQ SEQUENCE 547 AA; 60253 MW; 7428DDA39BFD0654 CRC64;
MGSIPSEKET IFRSKLPDIY VPDHLPLHSY CFQNLHQFSD RPCLIDGFTN KTLTYAEVEL
ASKRVGAGLH RLGLRQGHVV MLLLPNSIEF VLSFIGASLL GAMSTTANPF YTSAEIHKQA
AAAGAKIIVT ESCHVSKLQG LEGISRIVVI DDAVRVPENV MHFSELESTD EAELPRIDVH
PDDVVALPYS SGTTGLPKGV MLTHNGLVTS VAQQVDGENP NLHFSEDDVL LCVLPLFHIY
SLNSVLLCGL RAGAAIVLMR KFEIVRLMEL VEKYRVTIAP FVPPIVVEMV KNEAVDRYDL
SSIRVVMSGA APMGKELENK LREKLPNAKL GQGYGMTEAG PVLSMCLAFA KEPFEVKSGS
CGTVVRNAEL KIIDPETGFS LSRNQPGEIC IRGNQIMKGY LNNPEATKQT IDEEGWLHTG
DIGFVDDDDE IFIVDRLKEL IKYKGFQVAP AELEAMLITH PNMADAAVVS IKDDSCGELP
VAFIVRSNGS EITEDEIKKY ISKQVVFYKR IHRVFFIEAI PKAPSGKILR KELRARLAAE
CPNGRQL
