4CL1_ORYSJ
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 03-AUG-2022, entry version 135.
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=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). {ECO:0000269|PubMed:21807887,
CC 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 -!- 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; 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 RefSeq; XP_015650724.1; XM_015795238.1.
DR AlphaFoldDB; P17814; -.
DR SMR; P17814; -.
DR STRING; 4530.OS08T0245200-01; -.
DR PaxDb; P17814; -.
DR PRIDE; P17814; -.
DR EnsemblPlants; Os08t0245200-01; Os08t0245200-01; Os08g0245200.
DR GeneID; 4345054; -.
DR Gramene; Os08t0245200-01; Os08t0245200-01; Os08g0245200.
DR KEGG; osa:4345054; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; P17814; -.
DR OMA; THWTNIP; -.
DR OrthoDB; 683933at2759; -.
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; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; P17814; OS.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW 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..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 352..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
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
