4CL2_NARPS
ID 4CL2_NARPS Reviewed; 569 AA.
AC A0A2H5AIY4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=4-coumarate-CoA ligase 2 {ECO:0000303|PubMed:29229969};
DE EC=6.2.1.12 {ECO:0000250|UniProtKB:Q42524};
GN Name=4CL2 {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; MF416094; AUG71939.1; -; mRNA.
DR AlphaFoldDB; A0A2H5AIY4; -.
DR SMR; A0A2H5AIY4; -.
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..569
FT /note="4-coumarate-CoA ligase 2"
FT /id="PRO_0000450636"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..359
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 360..427
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 216..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 337..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 359..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
SQ SEQUENCE 569 AA; 60971 MW; DD7B5301E008E237 CRC64;
MITIAESHPQ IHHSPPDTTA PSTPPTATIF RSRLPDIVLS NHLPLHEYLF ENTLTSPSPC
IISASTGRSY SFAETHLLSR KTASFLSSRC GVRRGGVVML LLHNCPEFVF SFLGSSMLGA
VTTAANPFCT PQEIKKQLLA SGATVIITQS AYASKISRDD DVEDLIVVTV SDNELERHAA
PPEGCVSFSE VESADEDAVP DAVGVGPEDA VAMPFSSGTT GLPKGVVLTH KSMTSSVGQI
VDGENPNLHL RKGEDVLLCV LPLFHIFSLN SVLLCGLRTG AAVVIMARFE MEGMLETIQR
WGVSVAAVVP PLVLALAKNP LVEKYDMGTV RMVLSGAAPL GKELEAVLKG RLPQAVLGQG
YGMTEAGPVI SMSPGFAKQP TPVKSGSCGT VVRNAELKVM DPETGFSLGR NQPGEICVRG
PQIMKGYLND PEATSATIDV EGWLHTGDVG YVDDDDEVFI VDRVKELIKF KGFQVPPAEL
EALLLGHPSI ADAAVIPQND EVAGEVPVAF VVPSKSSDLT EEIVKEFISK QVVFYKRIHR
VYFIHAIPKS PSGKILRKDL RAKVASFSS
