Reviewed, UniProtKB/Swiss-Prot Q84P23 (4CLL9_ARATH)

Names and origin

Protein names

Recommended name:
    4-coumarate--CoA ligase-like 9
    EC=6.2.1.-
Alternative name(s):
    4-coumarate--CoA ligase isoform 4
      Short name=At4CL4

Gene names

Name:	4CLL9
Ordered Locus Names:	At5g63380
ORF Names:	K9H21.11, K9H21.8

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

General annotation (Comments)

Function	Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Converts 12-oxo-phytodienoic acid (OPDA) into OPDA-CoA. Ref.6
Subcellular location	Peroxisome. Ref.6
Domain	Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity By similarity.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=11 µM for OPDA

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Peroxisome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity 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 – 562	562	4-coumarate--CoA ligase-like 9		PRO_0000299182
Regions
	Nucleotide binding	212 – 220	9	ATP By similarity
	Nucleotide binding	353 – 358	6	ATP By similarity
	Region	283 – 352	70	SBD1 By similarity
	Region	353 – 417	65	SBD2 By similarity
	Motif	560 – 562	3	Microbody targeting signal Potential
Sites
	Binding site	438	1	ATP By similarity
	Binding site	453	1	ATP By similarity
	Binding site	544	1	ATP By similarity
Experimental info
	Sequence conflict	523	1	T → A in AAP03018. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q84P23-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: DE8E87063F2B2DB3	FASTA	562	61,278
	10 20 30 40 50 60 MLTKTNDSRL IDRSSGFDQR TGIYHSLRPS LSLPPIDQPL SAAEFALSLL LKSSPPATAG 70 80 90 100 110 120 KNIEALTYLV NSSSGDNLTY GELLRRVRSL AVSLRERFPS LASRNVAFIL SPSSLDIPVL 130 140 150 160 170 180 YLALMSIGVV VSPANPIGSE SEVSHQVEVS EPVIAFATSQ TVKKLQSSSL PLGTVLMDST 190 200 210 220 230 240 EFLSWLNRSD SSSVNPFQVQ VNQSDPAAIL FSSGTTGRVK GVLLTHRNLI ASTAVSHQRT 250 260 270 280 290 300 LQDPVNYDRV GLFSLPLFHV FGFMMMIRAI SLGETLVLLG RFELEAMFKA VEKYKVTGMP 310 320 330 340 350 360 VSPPLIVALV KSELTKKYDL RSLRSLGCGG APLGKDIAER FKQKFPDVDI VQGYGLTESS 370 380 390 400 410 420 GPAASTFGPE EMVKYGSVGR ISENMEAKIV DPSTGESLPP GKTGELWLRG PVIMKGYVGN 430 440 450 460 470 480 EKASAETVDK EGWLKTGDLC YFDSEDFLYI VDRLKELIKY KAYQVPPVEL EQILHSNPDV 490 500 510 520 530 540 IDAAVVPFPD EDAGEIPMAF IVRKPGSNLN EAQIIDFVAK QVTPYKKVRR VAFINAIPKN 550 560 PAGKILRREL TKIAVDGNAS KL

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 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [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]. Strain: cv. Columbia.
[5]	"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.
[6]	"A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid." Schneider K., Kienow L., Schmelzer E., Colby T., Bartsch M., Miersch O., Wasternack C., Kombrink E., Stuible H.-P. J. Biol. Chem. 280:13962-13972(2005) [PubMed: 15677481] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME ACTIVITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY250835 mRNA. Translation: AAP03018.1. AY376731 mRNA. Translation: AAQ86590.1. AB023035, AB007649 Genomic DNA. Translation: BAB10742.1. AY136459 mRNA. Translation: AAM97124.1. BT010394 mRNA. Translation: AAQ56837.1.
IPI	IPI00541683.
RefSeq	NP_201143.1.
UniGene	At.27966
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Proteomic databases
PRIDE	Q84P23.
Genome annotation databases
GeneID	836457.
GenomeReviews	Gene locus AT5G63380 in contig BA000015_GR.
KEGG	ath:AT5G63380.
NMPDR	fig|3702.1.peg.28385.
Organism-specific databases
TAIR	At5g63380.
Phylogenomic databases
OMA	Q84P23. RISENME.
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

4CLL9_ARATH

Accession

Primary (citable) accession number: Q84P23
Secondary accession number(s): Q9FGW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	June 16, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)