Q84P21 (4CLL5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-coumarate--CoA ligase-like 5
EC=6.2.1.-

Alternative name(s):
4-coumarate--CoA ligase isoform 9
Short name=At4CL9
Peroxisomal OPC-8:0-CoA ligase 1

Gene names

Name:	4CLL5
Synonyms:	OPCL1
Ordered Locus Names:	At1g20510
ORF Names:	F5M15.17

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	546 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. Converts 12-oxo-phytodienoic acid (OPDA) and 3-oxo-2-(2'-pentenyl)-cyclopentane-1-octanoic acid (OPC-8:0) into OPDA-CoA and OPC-8:0-CoA, respectively.
Subcellular location	Peroxisome Ref.2.
Induction	By wounding or by jasmonic acid (JA) treatment. Ref.2
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=24 µM for OPDA KM=47 µM for OPC-8:0
Sequence caution	The sequence AAF79611.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
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 mutant phenotype Ref.2. Source: TAIR response to wounding Inferred from expression pattern. Source: TAIR
Cellular component	peroxisome Inferred from direct assay Ref.2. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q84P21-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 546	546	4-coumarate--CoA ligase-like 5		PRO_0000299178
Regions
	Nucleotide binding	197 – 205	9	ATP By similarity
	Nucleotide binding	339 – 344	6	ATP By similarity
	Region	267 – 338	72	SBD1 By similarity
	Region	339 – 403	65	SBD2 By similarity
	Motif	544 – 546	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
Experimental info
	Sequence conflict	247	1	A → T in AAP03021. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 628BB0F1CD0AC9BE	FASTA	546	59,375
	10 20 30 40 50 60 MASVNSRSGF CNSNSTFYSK RTPIPLPPNP SLDVTTFISS QAHRGRIAFI DASTGQNLTF 70 80 90 100 110 120 TELWRAVESV ADCLSEIGIR KGHVVLLLSP NSILFPVVCL SVMSLGAIIT TTNPLNTSNE 130 140 150 160 170 180 IAKQIKDSNP VLAFTTSQLL PKISAAAKKL PIVLMDEERV DSVGDVRRLV EMMKKEPSGN 190 200 210 220 230 240 RVKERVDQDD TATLLYSSGT TGMSKGVISS HRNLIAMVQT IVNRFGSDDG EQRFICTVPM 250 260 270 280 290 300 FHIYGLAAFA TGLLAYGSTI IVLSKFEMHE MMSAIGKYQA TSLPLVPPIL VAMVNGADQI 310 320 330 340 350 360 KAKYDLSSMH TVLCGGAPLS KEVTEGFAEK YPTVKILQGY GLTESTGIGA STDTVEESRR 370 380 390 400 410 420 YGTAGKLSAS MEGRIVDPVT GQILGPKQTG ELWLKGPSIM KGYFSNEEAT SSTLDSEGWL 430 440 450 460 470 480 RTGDLCYIDE DGFIFVVDRL KELIKYKGYQ VAPAELEALL LTHPEITDAA VIPFPDKEVG 490 500 510 520 530 540 QFPMAYVVRK TGSSLSEKTI MEFVAKQVAP YKRIRKVAFV SSIPKNPSGK ILRKDLIKIA TSNSKL

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]	"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: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY250838 mRNA. Translation: AAP03021.1. EF014466 mRNA. Translation: ABJ98946.1. AC027665 Genomic DNA. Translation: AAF79611.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE29980.1. AF360250 mRNA. Translation: AAK25960.1. AY040047 mRNA. Translation: AAK64105.1.
IPI	IPI00533937.
RefSeq	NP_564115.1. NM_101901.3.
UniGene	At.15241.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q84P21.
SMR	Q84P21. Positions 21-545.
ModBase	Search...
Protein-protein interaction databases
STRING	Q84P21.
Proteomic databases
PRIDE	Q84P21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G20510.1; AT1G20510.1; AT1G20510.
GeneID	838639.
GenomeReviews	Gene locus AT1G20510 in contig CT485782_GR.
KEGG	ath:AT1G20510.
NMPDR	fig|3702.1.peg.2397.
Organism-specific databases
TAIR	At1g20510.
Phylogenomic databases
GeneTree	EPGT00070000028073.
HOGENOM	HBG547964.
InParanoid	Q84P21.
OMA	CARALYH.
PhylomeDB	Q84P21.
ProtClustDB	CLSN2679410.
Gene expression databases
Genevestigator	Q84P21.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K10526.
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

4CLL5_ARATH

Accession

Primary (citable) accession number: Q84P21
Secondary accession number(s): Q9C5H2, Q9LMV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	November 16, 2011
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program