ID 4CL2_SOLTU Reviewed; 545 AA.
AC P31685;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=4-coumarate--CoA ligase 2;
DE Short=4CL 2;
DE EC=6.2.1.12 {ECO:0000250|UniProtKB:O24146};
DE AltName: Full=4-coumaroyl-CoA synthase 2;
GN Name=4CL2; Synonyms=4CL-2;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2022667; DOI=10.1016/s0021-9258(18)93010-3;
RA Becker-Andre M., Schulze-Lefert P., Hahlbrock K.;
RT "Structural comparison, modes of expression, and putative cis-acting
RT elements of the two 4-coumarate: CoA ligase genes in potato.";
RL J. Biol. Chem. 266:8551-8559(1991).
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 -!- 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 PIR; B39827; B39827.
DR AlphaFoldDB; P31685; -.
DR SMR; P31685; -.
DR STRING; 4113.P31685; -.
DR PaxDb; 4113-PGSC0003DMT400036886; -.
DR eggNOG; KOG1176; Eukaryota.
DR InParanoid; P31685; -.
DR UniPathway; UPA00372; UER00547.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P31685; baseline.
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:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05904; 4CL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR24096:SF402; 4-COUMARATE--COA LIGASE 1; 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 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Nucleotide-binding;
KW Phenylpropanoid metabolism; Reference proteome.
FT CHAIN 1..545
FT /note="4-coumarate--CoA ligase 2"
FT /id="PRO_0000193037"
FT REGION 265..334
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 335..402
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
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 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 242
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 246
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 263
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 312
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 334
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 335
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 339
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 347
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 440
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 444
FT /ligand="(E)-4-coumaroyl-AMP"
FT /ligand_id="ChEBI:CHEBI:192348"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 446
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 447
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O24146"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O24146"
SQ SEQUENCE 545 AA; 59625 MW; 5481F0B0AFEA39E0 CRC64;
MPMDIETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE
VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV
KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSAPE GCVHFSELIQ SDEHEIPDVK
IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH
IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVHNY
DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS
GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH
TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE
VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA
AGISN
//
