4CL4_ARATH
ID 4CL4_ARATH Reviewed; 570 AA.
AC Q9LU36; Q84P22; Q8LPN8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=4-coumarate--CoA ligase 4;
DE Short=4CL 4;
DE EC=6.2.1.12;
DE AltName: Full=4-coumarate--CoA ligase isoform 5;
DE Short=At4CL5;
DE AltName: Full=4-coumaroyl-CoA synthase 4;
GN Name=4CL4; OrderedLocusNames=At3g21230; ORFNames=MXL8_9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY ORGANIZATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lawrence P.K.;
RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase
RT genes.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-570.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=14769935; DOI=10.1073/pnas.0307307101;
RA Hamberger B., Hahlbrock K.;
RT "The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana comprises
RT one rare, sinapate-activating and three commonly occurring isoenzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2209-2214(2004).
RN [7]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA Kombrink E., Stuible H.-P.;
RT "The substrate specificity-determining amino acid code of 4-coumarate:CoA
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN [8]
RP INDUCTION BY WOUNDING.
RX PubMed=16738863; DOI=10.1007/s00425-006-0296-y;
RA Soltani B.M., Ehlting J., Hamberger B., Douglas C.J.;
RT "Multiple cis-regulatory elements regulate distinct and complex patterns of
RT developmental and wound-induced expression of Arabidopsis thaliana 4CL gene
RT family members.";
RL Planta 224:1226-1238(2006).
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:0000269|PubMed:14769935}.
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:14769935};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=432 uM for 4-coumarate;
CC KM=186 uM for caffeate;
CC KM=26 uM for ferulate;
CC KM=20 uM for sinapate;
CC Vmax=100 nmol/sec/mg enzyme with 4-coumarate as substrate;
CC Vmax=187 nmol/sec/mg enzyme with caffeate as substrate;
CC Vmax=153 nmol/sec/mg enzyme with ferulate as substrate;
CC Vmax=105 nmol/sec/mg enzyme with sinapate as substrate;
CC -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC 1/2.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:16738863}.
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}.
CC -!- MISCELLANEOUS: Activates efficiently sinapate, besides the usual 4CL
CC substrates (4-coumarate, caffeate, and ferulate).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM19949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY250837; AAP03020.1; -; mRNA.
DR EMBL; AY376732; AAQ86591.1; -; mRNA.
DR EMBL; AB023045; BAB01715.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76479.1; -; Genomic_DNA.
DR EMBL; AY095992; AAM19949.1; ALT_INIT; mRNA.
DR EMBL; BT000614; AAN18181.1; -; mRNA.
DR RefSeq; NP_188760.3; NM_113018.4.
DR AlphaFoldDB; Q9LU36; -.
DR SMR; Q9LU36; -.
DR STRING; 3702.AT3G21230.1; -.
DR PaxDb; Q9LU36; -.
DR PRIDE; Q9LU36; -.
DR ProteomicsDB; 244518; -.
DR EnsemblPlants; AT3G21230.1; AT3G21230.1; AT3G21230.
DR GeneID; 821677; -.
DR Gramene; AT3G21230.1; AT3G21230.1; AT3G21230.
DR KEGG; ath:AT3G21230; -.
DR Araport; AT3G21230; -.
DR TAIR; locus:2094771; AT3G21230.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q9LU36; -.
DR OMA; VDGWFCT; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q9LU36; -.
DR BRENDA; 6.2.1.12; 399.
DR SABIO-RK; Q9LU36; -.
DR UniPathway; UPA00372; UER00547.
DR PRO; PR:Q9LU36; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU36; baseline and differential.
DR Genevisible; Q9LU36; AT.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:TAIR.
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..570
FT /note="4-coumarate--CoA ligase 4"
FT /id="PRO_0000193030"
FT REGION 291..360
FT /note="SBD1"
FT /evidence="ECO:0000250"
FT REGION 361..427
FT /note="SBD2"
FT /evidence="ECO:0000250"
FT BINDING 218..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 361..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 81
FT /note="T -> I (in Ref. 1; AAP03020)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> T (in Ref. 1; AAP03020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62559 MW; 2C2CB71BD5F5860A CRC64;
MVLQQQTHFL TKKIDQEDEE EEPSHDFIFR SKLPDIFIPN HLPLTDYVFQ RFSGDGDGDS
STTCIIDGAT GRILTYADVQ TNMRRIAAGI HRLGIRHGDV VMLLLPNSPE FALSFLAVAY
LGAVSTTANP FYTQPEIAKQ AKASAAKMII TKKCLVDKLT NLKNDGVLIV CLDDDGDNGV
VSSSDDGCVS FTELTQADET ELLKPKISPE DTVAMPYSSG TTGLPKGVMI THKGLVTSIA
QKVDGENPNL NFTANDVILC FLPMFHIYAL DALMLSAMRT GAALLIVPRF ELNLVMELIQ
RYKVTVVPVA PPVVLAFIKS PETERYDLSS VRIMLSGAAT LKKELEDAVR LKFPNAIFGQ
GYGMTESGTV AKSLAFAKNP FKTKSGACGT VIRNAEMKVV DTETGISLPR NKSGEICVRG
HQLMKGYLND PEATARTIDK DGWLHTGDIG FVDDDDEIFI VDRLKELIKF KGYQVAPAEL
EALLISHPSI DDAAVVAMKD EVADEVPVAF VARSQGSQLT EDDVKSYVNK QVVHYKRIKM
VFFIEVIPKA VSGKILRKDL RAKLETMCSK
