Q9M0X9 (4CLL7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-coumarate--CoA ligase-like 7
EC=6.2.1.-

Alternative name(s):
4-coumarate--CoA ligase isoform 6
Short name=At4CL6

Gene names

Name:	4CLL7
Ordered Locus Names:	At4g05160
ORF Names:	C17L7.80

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	544 AA.
Sequence status	Complete.
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. Ref.6
Subcellular location	Peroxisome Ref.6.
Induction	By methyl jasmonate. 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=9 µM for nonanoic acid

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Oxylipin biosynthesis
Cellular component	Peroxisome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	jasmonic acid biosynthetic process Inferred from direct assay Ref.6. Source: TAIR oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	peroxisome Inferred from direct assay Ref.6PubMed 17951448. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fatty-acyl-CoA synthase activity Inferred from direct assay Ref.6. Source: TAIR 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 – 544	544	4-coumarate--CoA ligase-like 7		PRO_0000299180
Regions
	Nucleotide binding	198 – 206	9	ATP By similarity
	Nucleotide binding	339 – 344	6	ATP By similarity
	Region	269 – 338	70	SBD1 By similarity
	Region	339 – 403	65	SBD2 By similarity
	Motif	542 – 544	3	Microbody targeting signal Potential
Sites
	Binding site	424	1	ATP By similarity
	Binding site	439	1	ATP By similarity
	Binding site	530	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9M0X9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B2422848E70D2909	FASTA	544	59,850
	10 20 30 40 50 60 MEKSGYGRDG IYRSLRPTLV LPKDPNTSLV SFLFRNSSSY PSKLAIADSD TGDSLTFSQL 70 80 90 100 110 120 KSAVARLAHG FHRLGIRKND VVLIFAPNSY QFPLCFLAVT AIGGVFTTAN PLYTVNEVSK 130 140 150 160 170 180 QIKDSNPKII ISVNQLFDKI KGFDLPVVLL GSKDTVEIPP GSNSKILSFD NVMELSEPVS 190 200 210 220 230 240 EYPFVEIKQS DTAALLYSSG TTGTSKGVEL THGNFIAASL MVTMDQDLMG EYHGVFLCFL 250 260 270 280 290 300 PMFHVFGLAV ITYSQLQRGN ALVSMARFEL ELVLKNIEKF RVTHLWVVPP VFLALSKQSI 310 320 330 340 350 360 VKKFDLSSLK YIGSGAAPLG KDLMEECGRN IPNVLLMQGY GMTETCGIVS VEDPRLGKRN 370 380 390 400 410 420 SGSAGMLAPG VEAQIVSVET GKSQPPNQQG EIWVRGPNMM KGYLNNPQAT KETIDKKSWV 430 440 450 460 470 480 HTGDLGYFNE DGNLYVVDRI KELIKYKGFQ VAPAELEGLL VSHPDILDAV VIPFPDEEAG 490 500 510 520 530 540 EVPIAFVVRS PNSSITEQDI QKFIAKQVAP YKRLRRVSFI SLVPKSAAGK ILRRELVQQV RSKM

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION. Strain: cv. Wassilewskija.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY250839 mRNA. Translation: AAP03022.1. AL161502 Genomic DNA. Translation: CAB81058.1. CP002687 Genomic DNA. Translation: AEE82486.1. AY091079 mRNA. Translation: AAM13899.1. AY122950 mRNA. Translation: AAM67483.1.
IPI	IPI00536809.
PIR	H85064.
RefSeq	NP_192425.1. NM_116755.4.
UniGene	At.33913.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q9M0X9.
SMR	Q9M0X9. Positions 12-536.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G05160.1-P.
Proteomic databases
PaxDb	Q9M0X9.
PRIDE	Q9M0X9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G05160.1; AT4G05160.1; AT4G05160.
GeneID	825864.
KEGG	ath:AT4G05160.
Organism-specific databases
TAIR	At4g05160.
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000230009.
InParanoid	Q9M0X9.
KO	K01904.
OMA	TTRFAER.
PhylomeDB	Q9M0X9.
ProtClustDB	CLSN2685605.
Gene expression databases
Genevestigator	Q9M0X9.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

4CLL7_ARATH

Accession

Primary (citable) accession number: Q9M0X9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program