ID   4CL1_ORYSJ              Reviewed;         564 AA.
AC   P17814; B7EH38; Q0J6Z8; Q6ZKV9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   04-NOV-2026, entry version 151.
DE   RecName: Full=4-coumarate--CoA ligase 1 {ECO:0000303|PubMed:18627494};
DE            Short=4CL 1 {ECO:0000303|PubMed:18627494};
DE            Short=Os4CL1 {ECO:0000303|PubMed:18627494};
DE            EC=6.2.1.12 {ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
DE   AltName: Full=(E)-ferulate--CoA ligase {ECO:0000305};
DE            EC=6.2.1.34 {ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
DE   AltName: Full=4-coumaroyl-CoA synthase 1 {ECO:0000305};
GN   Name=4CL1 {ECO:0000303|PubMed:18627494}; Synonyms=4CL {ECO:0000305};
GN   OrderedLocusNames=Os08g0245200 {ECO:0000312|EMBL:BAT04523.1},
GN   LOC_Os08g14760 {ECO:0000305};
GN   ORFNames=OJ1033_B09.16 {ECO:0000312|EMBL:BAD05189.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2235510; DOI=10.1093/nar/18.20.6144;
RA   Zhao Y., Kung S.D., Dube S.K.;
RT   "Nucleotide sequence of rice 4-coumarate:CoA ligase gene, 4-CL.1.";
RL   Nucleic Acids Res. 18:6144-6144(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=18627494; DOI=10.1111/j.1469-8137.2008.02534.x;
RA   de Azevedo Souza C., Barbazuk B., Ralph S.G., Bohlmann J., Hamberger B.,
RA   Douglas C.J.;
RT   "Genome-wide analysis of a land plant-specific acyl:coenzyme A synthetase
RT   (ACS) gene family in Arabidopsis, poplar, rice and Physcomitrella.";
RL   New Phytol. 179:987-1003(2008).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=21807887; DOI=10.1104/pp.111.178301;
RA   Gui J., Shen J., Li L.;
RT   "Functional characterization of evolutionarily divergent 4-
RT   coumarate:coenzyme a ligases in rice.";
RL   Plant Physiol. 157:574-586(2011).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=23246835; DOI=10.1016/j.bbrc.2012.12.019;
RA   Sun H., Li Y., Feng S., Zou W., Guo K., Fan C., Si S., Peng L.;
RT   "Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and
RT   stress response for potential roles in lignin and flavonoid biosynthesis in
RT   rice.";
RL   Biochem. Biophys. Res. Commun. 430:1151-1156(2013).
CC   -!- FUNCTION: Involved in the phenylpropanoid metabolism by mediating the
CC       activation of a number of hydroxycinnamates for the biosynthesis of
CC       monolignols and other phenolic secondary metabolites (PubMed:21807887,
CC       PubMed:23246835). Catalyzes the formation of CoA esters of cinnamate,
CC       4-coumarate, caffeate and ferulate (PubMed:21807887, PubMed:23246835).
CC       Is more efficient with substrates in the following order: ferulate > 4-
CC       coumarate > cinnamate > caffeate (PubMed:21807887). Cannot convert
CC       sinapate to its corresponding CoA ester (PubMed:21807887,
CC       PubMed:23246835). 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 (By similarity). {ECO:0000250|UniProtKB:O24146,
CC       ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:87305, ChEBI:CHEBI:456215; EC=6.2.1.34;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36252;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
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:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:64788, ChEBI:CHEBI:15669,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57252,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64789;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770,
CC         ChEBI:CHEBI:87136, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300;
CC         Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-ferulate + ATP + H(+) = (E)-feruloyl-AMP + diphosphate;
CC         Xref=Rhea:RHEA:72439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29749,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192350;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72440;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-feruloyl-AMP + CoA = (E)-feruloyl-CoA + AMP + H(+);
CC         Xref=Rhea:RHEA:72443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:87305, ChEBI:CHEBI:192350, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72444;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
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:0000305|PubMed:21807887,
CC         ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
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:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeate + ATP + H(+) = (E)-caffeoyl-AMP + diphosphate;
CC         Xref=Rhea:RHEA:72431, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57770, ChEBI:CHEBI:192349;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72432;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoyl-AMP + CoA = (E)-caffeoyl-CoA + AMP + H(+);
CC         Xref=Rhea:RHEA:72435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:87136, ChEBI:CHEBI:192349, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72436;
CC         Evidence={ECO:0000305|PubMed:21807887, ECO:0000305|PubMed:23246835};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O24146};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.4 uM for cinnamate {ECO:0000269|PubMed:21807887};
CC         KM=11.9 uM for 4-coumarate {ECO:0000269|PubMed:21807887};
CC         KM=29.3 uM for caffeate {ECO:0000269|PubMed:21807887};
CC         KM=8.3 uM for ferulate {ECO:0000269|PubMed:21807887};
CC         Vmax=100 pmol/sec/mg enzyme with cinnamate as substrate
CC         {ECO:0000269|PubMed:21807887};
CC         Vmax=130 pmol/sec/mg enzyme with 4-coumarate as substrate
CC         {ECO:0000269|PubMed:21807887};
CC         Vmax=140 pmol/sec/mg enzyme with caffeate as substrate
CC         {ECO:0000269|PubMed:21807887};
CC         Vmax=110 pmol/sec/mg enzyme with ferulate as substrate
CC         {ECO:0000269|PubMed:21807887};
CC         Note=kcat is 0.37 min(-1) with cinnamate as substrate
CC         (PubMed:21807887). kcat is 0.49 min(-1) with 4-coumarate as substrate
CC         (PubMed:21807887). kcat is 0.52 min(-1) with caffeate as substrate
CC         (PubMed:21807887). kcat is 0.41 min(-1) with ferulate as substrate
CC         (PubMed:21807887). {ECO:0000269|PubMed:21807887};
CC   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       1/2. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaf blades and leaf
CC       sheaths. {ECO:0000269|PubMed:21807887}.
CC   -!- INDUCTION: Induced by fungal elicitor and UV irradiation. Down-
CC       regulated by wounding and UV irradiation (PubMed:23246835).
CC       {ECO:0000269|PubMed:23246835}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD05189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA36850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA36850.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X52623; CAA36850.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP003859; BAD05189.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008214; BAF23267.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04523.1; -; Genomic_DNA.
DR   EMBL; AK069932; BAG91685.1; -; mRNA.
DR   PIR; JU0311; JU0311.
DR   AlphaFoldDB; P17814; -.
DR   SMR; P17814; -.
DR   FunCoup; P17814; 1518.
DR   STRING; 39947.P17814; -.
DR   PaxDb; 39947-P17814; -.
DR   EnsemblPlants; Os08t0245200-01; Os08t0245200-01; Os08g0245200.
DR   Gramene; Os08t0245200-01; Os08t0245200-01; Os08g0245200.
DR   KEGG; dosa:Os08g0245200; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_2_1; -.
DR   InParanoid; P17814; -.
DR   OMA; ACDAPII; -.
DR   OrthoDB; 1898221at2759; -.
DR   BRENDA; 6.2.1.12; 4460.
DR   PlantReactome; R-OSA-1119316; Phenylpropanoid biosynthesis.
DR   PlantReactome; R-OSA-1119418; Suberin biosynthesis.
DR   PlantReactome; R-OSA-1119531; Flavonoid biosynthesis.
DR   UniPathway; UPA00372; UER00547.
DR   Proteomes; UP000059680; Chromosome 8.
DR   GO; GO:0106286; F:(E)-caffeate-CoA ligase activity; EXP:UniProtKB.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0050563; F:trans-feruloyl-CoA synthase activity; EXP:UniProtKB.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB.
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:SF217; 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   1: Evidence at protein level;
KW   ATP-binding; Ligase; Magnesium; Nucleotide-binding;
KW   Phenylpropanoid metabolism; Reference proteome.
FT   CHAIN           1..564
FT                   /note="4-coumarate--CoA ligase 1"
FT                   /id="PRO_0000193031"
FT   REGION          282..351
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          352..419
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         259
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         263
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         280
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         329
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         351
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         352
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         356
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         364
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         455
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         457
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         461
FT                   /ligand="(E)-4-coumaroyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:192348"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         463
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         464
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O24146"
FT   CONFLICT        405
FT                   /note="P -> R (in Ref. 1; CAA36850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="I -> N (in Ref. 1; CAA36850)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  60902 MW;  9725A4B4A72F8C6E CRC64;
     MGSMEQQQPE SAAPATEASP EIIFRSKLQD IAITNTLPLH RYCFERLPEV AARPCLIDGA
     TGGVLTYADV DRLSRRLAAA LRRAPLGLRR GGVVMSLLRN SPEFVLSFFA ASRVGAAVTT
     ANPMSTPHEI ESQLAAAGAT VVITESMAAD KLPSHSHGAL TVVLIDERRD GCLHFWDDLM
     SEDEASPLAG DEDDEKVFDP DDVVALPYSS GTTGLPKGVM LTHRSLSTSV AQQVDGENPN
     IGLHAGDVIL CALPMFHIYS LNTIMMCGLR VGAAIVVMRR FDLAAMMDLV ERHRVTIAPL
     VPPIVVAVAK SEAAAARDLS SVRMVLSGAA PMGKDIEDAF MAKLPGAVLG QGYGMTEAGP
     VLSMCLAFAK EPFKVKSGAC GTVVRNAELK IIDPDTGKSL GRNLPGEICI RGQQIMKGYL
     NNPEATKNTI DAEGWLHTGD IGYVDDDDEI FIVDRLKEII KYRGFQVAPA ELEALLITHP
     SIADAAVVGK QIEPEIGEIP VAFVAKTEGS ELSEDDVKQF VAKEVIYYKK IREVFFVDKI
     PKAPSGKILR KELRKQLQHL QQEA
//