Reviewed, UniProtKB/Swiss-Prot Q3E6Y4 (4CLL3_ARATH)

Names and origin

Protein names

Recommended name:
    4-coumarate--CoA ligase-like 3
    EC=6.2.1.-

Gene names

Name:	4CLL3
Ordered Locus Names:	At1g20490
ORF Names:	F5M15.30

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	552 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.5
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 AAF79612.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 3 genes: At1g20480, At1g20490 and At1g20500. The sequence AAF79612.1 differs from that shown. Reason: Frameshift at position 431. The sequence BX815999 differs from that shown. Reason: Miscellaneous discrepancy. Sequencing errors.

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 – 552	552	4-coumarate--CoA ligase-like 3		PRO_0000299176
Regions
	Nucleotide binding	207 – 215	9	ATP By similarity
	Nucleotide binding	347 – 352	6	ATP By similarity
	Region	275 – 346	72	SBD1 By similarity
	Region	347 – 411	65	SBD2 By similarity
	Motif	550 – 552	3	Microbody targeting signal Potential
Sites
	Binding site	432	1	ATP By similarity
	Binding site	447	1	ATP By similarity
	Binding site	538	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3E6Y4-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 8E4D96B2645B6254	FASTA	552	60,499
	10 20 30 40 50 60 MAYPERDLIV DPRSGFCKSN STFYSKRNPL CLPPNPSLDV TTFISSQPQR GTTAFIDAST 70 80 90 100 110 120 GHRLTFSDLW RVVDRVADCL YHEVGIRRGD VVLILSPNSI YIPVVCLSVM SLGAVVTTAN 130 140 150 160 170 180 TLNTSGEISK QIAQSNPTLV FTTSQLAPKL AAAISVVLTD EEDEKRVELT SGVRVVGILS 190 200 210 220 230 240 EMMKKETSGQ RVRDRVNQDD TAMMLYSSGT TGTSKGVISS HRNLTAYVAK YIDDKWKRDE 250 260 270 280 290 300 IFVCTVPMFH SFGLLAFAMG SVASGSTVVI LRRFGLDDMM QAVEKYKATI LSLAPPVLVA 310 320 330 340 350 360 MINGADQLKA KYDLTSLRKV RCGGAPLSKE VMDSFLEKYP TVNIFQGYAL TESHGSGAST 370 380 390 400 410 420 ESVEESLKYG AVGLLSSGIE ARIVDPDTGR VMGVNQPGEL WLKGPSISKG YFGNEEATNE 430 440 450 460 470 480 TINLEGWLKL GDLCYIDEDG FLFVVDRLKE LIKYKGYQVP PAELEALLIA HPHILDAAVI 490 500 510 520 530 540 PFPDREAGQY PMAYVARKPE SNLSEKEVID FISNQVAPYK KIRKVAFISS IPKTASGKTL 550 RKDLIKLSTS KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation." Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M. Genome Res. 14:406-413(2004) [PubMed: 14993207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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: GENE FAMILY ORGANIZATION.
[4]	"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.
[5]	"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	AC027665 Genomic DNA. Translation: AAF79612.1. Sequence problems. BX815999 mRNA. No translation available.
IPI	IPI00524943.
PIR	D86338.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q3E6Y4.
Genome annotation databases
GenomeReviews	Gene locus AT1G20490 in contig CT485782_GR.
Organism-specific databases
TAIR	At1g20490.
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

4CLL3_ARATH

Accession

Primary (citable) accession number: Q3E6Y4
Secondary accession number(s): Q9LMV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	June 16, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)