Reviewed, UniProtKB/Swiss-Prot Q84P26 (4CLL8_ARATH)

Names and origin

Protein names

Recommended name:
    4-coumarate--CoA ligase-like 8
    EC=6.2.1.-
Alternative name(s):
    4-coumarate--CoA ligase isoform 11
      Short name=At4CL11

Gene names

Name:	4CLL8
Ordered Locus Names:	At5g38120
ORF Names:	MXA21.23, MXA21_10

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

General annotation (Comments)

Subcellular location	Peroxisome Potential.
Induction	By wounding or by jasmonic acid (JA) treatment. 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.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence BAB11279.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
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 – 550	550	4-coumarate--CoA ligase-like 8		PRO_0000299181
Regions
	Nucleotide binding	207 – 215	9	ATP By similarity
	Nucleotide binding	348 – 353	6	ATP By similarity
	Region	276 – 347	72	SBD1 By similarity
	Region	348 – 412	65	SBD2 By similarity
	Motif	548 – 550	3	Microbody targeting signal Potential
Sites
	Binding site	430	1	ATP By similarity
	Binding site	445	1	ATP By similarity
	Binding site	536	1	ATP By similarity
Experimental info
	Sequence conflict	72	1	M → R in AAP03015. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q84P26-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: F1E2D4A82864C623	FASTA	550	60,393
	10 20 30 40 50 60 MANSQRSSSL IDPRNGFCTS NSTFYSKRKP LALPSKESLD ITTFISSQTY RGKTAFIDAA 70 80 90 100 110 120 TDHRISFSDL WMAVDRVADC LLHDVGIRRG DVVLVLSPNT ISIPIVCLSV MSLGAVLTTA 130 140 150 160 170 180 NPLNTASEIL RQIADSNPKL AFTTPELAPK IASSGISIVL ERVEDTLRVP RGLKVVGNLT 190 200 210 220 230 240 EMMKKEPSGQ AVRNQVHKDD TAMLLYSSGT TGRSKGVNSS HGNLIAHVAR YIAEPFEQPQ 250 260 270 280 290 300 QTFICTVPLF HTFGLLNFVL ATLALGTTVV ILPRFDLGEM MAAVEKYRAT TLILVPPVLV 310 320 330 340 350 360 TMINKADQIM KKYDVSFLRT VRCGGAPLSK EVTQGFMKKY PTVDVYQGYA LTESNGAGAS 370 380 390 400 410 420 IESVEESRRY GAVGLLSCGV EARIVDPNTG QVMGLNQTGE LWLKGPSIAK GYFRNEEEII 430 440 450 460 470 480 TSEGWLKTGD LCYIDNDGFL FIVDRLKELI KYKGYQVPPA ELEALLLNHP DILDAAVIPF 490 500 510 520 530 540 PDKEAGQFPM AYVARKPESN LCEKKVIDFI SKQVAPYKKI RKVAFIDSIP KTPSGKTLRK 550 DLIKFAISKI

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. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed: 9330910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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.
[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]	"Identification of a peroxisomal acyl-activating enzyme involved in the biosynthesis of jasmonic acid in Arabidopsis." Koo A.J.K., Chung H.S., Kobayashi Y., Howe G.A. J. Biol. Chem. 281:33511-33520(2006) [PubMed: 16963437] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY250832 mRNA. Translation: AAP03015.1. AY376735 mRNA. Translation: AAQ86594.1. AB005247 Genomic DNA. Translation: BAB11279.1. Sequence problems. AK118041 mRNA. Translation: BAC42672.1. BT005689 mRNA. Translation: AAO64109.1.
IPI	IPI00541377.
RefSeq	NP_198628.2.
UniGene	At.30435
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Genome annotation databases
GeneID	833792.
GenomeReviews	Gene locus AT5G38120 in contig BA000015_GR.
KEGG	ath:AT5G38120.
NMPDR	fig|3702.1.peg.25499.
Organism-specific databases
TAIR	At5g38120.
Phylogenomic databases
OMA	Q84P26. NARELAF.
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

4CLL8_ARATH

Accession

Primary (citable) accession number: Q84P26
Secondary accession number(s): Q8GXU2, Q9FF44

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	June 16, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)