Reviewed, UniProtKB/Swiss-Prot Q9LU36 (4CL4_ARATH)

Names and origin

Protein names

Recommended name:
    4-coumarate--CoA ligase 4
      Short name=4CL 4
    EC=6.2.1.12
Alternative name(s):
    4-coumarate--CoA ligase isoform 5
      Short name=At4CL5
    4-coumaroyl-CoA synthase 4

Gene names

Name:	4CL4
Ordered Locus Names:	At3g21230
ORF Names:	MXL8_9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Produces CoA thioesters of a variety of hydroxy- and methoxy-substituted cinnamic acids, which are used to synthesize several phenylpropanoid-derived compounds, including anthocyanins, flavonoids, isoflavonoids, coumarins, lignin, suberin and wall-bound phenolics. Ref.5
Catalytic activity	ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA. Ref.5
Pathway	Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from 4-coumaric acid: step 1/2.
Induction	By wounding. Ref.7
Domain	Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity By similarity.
Miscellaneous	Activates efficiently sinapate, besides the usual 4CL substrates (4-coumarate, caffeate, and ferulate).
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=432 µM for 4-coumarate KM=186 µM for caffeate KM=26 µM for ferulate KM=20 µM for sinapate Vmax=100 nmol/sec/mg enzyme with 4-coumarate as substrate Vmax=187 nmol/sec/mg enzyme with caffeate as substrate Vmax=153 nmol/sec/mg enzyme with ferulate as substrate Vmax=105 nmol/sec/mg enzyme with sinapate as substrate

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phenylpropanoid biosynthetic process Inferred from direct assay. Source: TAIR
Molecular function	4-coumarate-CoA ligase activity Ref.5 Inferred from direct assay. Source: TAIR ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	4-coumarate--CoA ligase 4		PRO_0000193030
Regions
	Nucleotide binding	218 – 226	9	ATP By similarity
	Nucleotide binding	361 – 366	6	ATP By similarity
	Region	291 – 360	70	SBD1 By similarity
	Region	361 – 427	67	SBD2 By similarity
Sites
	Binding site	448	1	ATP By similarity
	Binding site	463	1	ATP By similarity
	Binding site	554	1	ATP By similarity
Experimental info
	Sequence conflict	81	1	T → I in AAP03020. Ref.1
	Sequence conflict	88	1	A → T in AAP03020. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9LU36-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2C2CB71BD5F5860A	FASTA	570	62,559
	10 20 30 40 50 60 MVLQQQTHFL TKKIDQEDEE EEPSHDFIFR SKLPDIFIPN HLPLTDYVFQ RFSGDGDGDS 70 80 90 100 110 120 STTCIIDGAT GRILTYADVQ TNMRRIAAGI HRLGIRHGDV VMLLLPNSPE FALSFLAVAY 130 140 150 160 170 180 LGAVSTTANP FYTQPEIAKQ AKASAAKMII TKKCLVDKLT NLKNDGVLIV CLDDDGDNGV 190 200 210 220 230 240 VSSSDDGCVS FTELTQADET ELLKPKISPE DTVAMPYSSG TTGLPKGVMI THKGLVTSIA 250 260 270 280 290 300 QKVDGENPNL NFTANDVILC FLPMFHIYAL DALMLSAMRT GAALLIVPRF ELNLVMELIQ 310 320 330 340 350 360 RYKVTVVPVA PPVVLAFIKS PETERYDLSS VRIMLSGAAT LKKELEDAVR LKFPNAIFGQ 370 380 390 400 410 420 GYGMTESGTV AKSLAFAKNP FKTKSGACGT VIRNAEMKVV DTETGISLPR NKSGEICVRG 430 440 450 460 470 480 HQLMKGYLND PEATARTIDK DGWLHTGDIG FVDDDDEIFI VDRLKELIKF KGYQVAPAEL 490 500 510 520 530 540 EALLISHPSI DDAAVVAMKD EVADEVPVAF VARSQGSQLT EDDVKSYVNK QVVHYKRIKM 550 560 570 VFFIEVIPKA VSGKILRKDL RAKLETMCSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases." Shockey J.M., Fulda M.S., Browse J. Plant Physiol. 132:1065-1076(2003) [PubMed: 12805634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION. Strain: cv. Wassilewskija.
[2]	"Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase genes." Lawrence P.K. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-570. Strain: cv. Columbia.
[5]	"The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapate-activating and three commonly occurring isoenzymes." Hamberger B., Hahlbrock K. Proc. Natl. Acad. Sci. U.S.A. 101:2209-2214(2004) [PubMed: 14769935] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[6]	"The substrate specificity-determining amino acid code of 4-coumarate:CoA ligase." Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D., Kombrink E., Stuible H.-P. Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003) [PubMed: 12819348] [Abstract] Cited for: GENE FAMILY ORGANIZATION.
[7]	"Multiple cis-regulatory elements regulate distinct and complex patterns of developmental and wound-induced expression of Arabidopsis thaliana 4CL gene family members." Soltani B.M., Ehlting J., Hamberger B., Douglas C.J. Planta 224:1226-1238(2006) [PubMed: 16738863] [Abstract] Cited for: INDUCTION BY WOUNDING.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY250837 mRNA. Translation: AAP03020.1. AY376732 mRNA. Translation: AAQ86591.1. AB023045 Genomic DNA. Translation: BAB01715.1. AY095992 mRNA. Translation: AAM19949.1. Different initiation. BT000614 mRNA. Translation: AAN18181.1.
IPI	IPI00521963.
RefSeq	NP_188760.3.
UniGene	At.38095
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Proteomic databases
PRIDE	Q9LU36.
Genome annotation databases
GeneID	821677.
GenomeReviews	Gene locus AT3G21230 in contig BA000014_GR.
KEGG	ath:AT3G21230.
NMPDR	fig|3702.1.peg.14357.
Organism-specific databases
TAIR	At3g21230.
Phylogenomic databases
OMA	Q9LU36. WIATEDF.
Enzyme and pathway databases
BRENDA	6.2.1.12. 302.
Gene expression databases
ArrayExpress	Q9LU36.
GermOnline	AT3G21230. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

4CL4_ARATH

Accession

Primary (citable) accession number: Q9LU36
Secondary accession number(s): Q84P22, Q8LPN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)