Q8LKS5 (LACS7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long chain acyl-CoA synthetase 7, peroxisomal
EC=6.2.1.3

Gene names

Name:	LACS7
Ordered Locus Names:	At5g27600
ORF Names:	F15A18.60

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	700 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate. Displays redundant function with LACS7 into the seed development process By similarity. Ref.7
Catalytic activity	ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1 Ref.5
Cofactor	Magnesium By similarity.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Interacts with PEX5. Ref.8
Subcellular location	Peroxisome Ref.5.
Tissue specificity	Preferentially expressed in seeds. Ref.8
Developmental stage	Induced during seed germination. Ref.5
Induction	Up-regulated by ozone and salt. Ref.8
Disruption phenotype	Seedlings of the double mutant lacs6/lacs7 were arrested in postgerminative growth due to inability to mobilize fatty acids into beta-oxidation, a necessary process to pursue the development. Ref.7
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence BAC43213.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to ozone Inferred from expression pattern Ref.8. Source: TAIR response to salt stress Inferred from expression pattern Ref.8. Source: TAIR
Cellular_component	peroxisome Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from direct assay Ref.1Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PEX5	Q9FMA3	4	EBI-993851,EBI-993861

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Long chain acyl-CoA synthetase 7, peroxisomal		PRO_0000401416
Regions
	Nucleotide binding	266 – 277	12	ATP Potential
	Region	526 – 550	25	Fatty acid-binding Potential
	Motif	10 – 18	9	Microbody targeting signal Potential
	Motif	698 – 700	3	Microbody targeting signal Potential
Experimental info
	Sequence conflict	657	1	F → L in AAM28874. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8LKS5 [UniParc]. Last modified November 30, 2010. Version 2. Checksum: EAD95B9F50DA75DB	FASTA	700	77,353
	10 20 30 40 50 60 MEFASPEQRR LETIRSHIDT SPTNDQSSSL FLNATASSAS PFFKEDSYSV VLPEKLDTGK 70 80 90 100 110 120 WNVYRSKRSP TKLVSRFPDH PEIGTLHDNF VHAVETYAEN KYLGTRVRSD GTIGEYSWMT 130 140 150 160 170 180 YGEAASERQA IGSGLLFHGV NQGDCVGLYF INRPEWLVVD HACAAYSFVS VPLYDTLGPD 190 200 210 220 230 240 AVKFVVNHAN LQAIFCVPQT LNILLSFLAE IPSIRLIVVV GGADEHLPSL PRGTGVTIVS 250 260 270 280 290 300 YQKLLSQGRS SLHPFSPPKP EDIATICYTS GTTGTPKGVV LTHGNLIANV AGSSVEAEFF 310 320 330 340 350 360 PSDVYISYLP LAHIYERANQ IMGVYGGVAV GFYQGDVFKL MDDFAVLRPT IFCSVPRLYN 370 380 390 400 410 420 RIYDGITSAV KSSGVVKKRL FEIAYNSKKQ AIINGRTPSA FWDKLVFNKI KEKLGGRVRF 430 440 450 460 470 480 MGSGASPLSP DVMDFLRICF GCSVREGYGM TETSCVISAM DDGDNLSGHV GSPNPACEVK 490 500 510 520 530 540 LVDVPEMNYT SDDQPYPRGE ICVRGPIIFK GYYKDEEQTR EILDGDGWLH TGDIGLWLPG 550 560 570 580 590 600 GRLKIIDRKK NIFKLAQGEY IAPEKIENVY TKCRFVSQCF IHGDSFNSSL VAIVSVDPEV 610 620 630 640 650 660 MKDWAASEGI KYEHLGQLCN DPRVRKTVLA EMDDLGREAQ LRGFEFAKAV TLVPEPFTLE 670 680 690 700 NGLLTPTFKI KRPQAKAYFA EAISKMYAEI AASNPIPSKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that participate in fatty acid and glycerolipid metabolism." Shockey J.M., Fulda M.S., Browse J.A. Plant Physiol. 129:1710-1722(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, ENZYME ACTIVITY.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [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]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-700. Strain: cv. Columbia.
[5]	"Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation." Fulda M., Shockey J., Werber M., Wolter F.P., Heinz E. Plant J. 32:93-103(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, ENZYME ACTIVITY.
[6]	"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: GENE FAMILY ORGANIZATION.
[7]	"Peroxisomal Acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana." Fulda M., Schnurr J., Abbadi A., Heinz E., Browse J. Plant Cell 16:394-405(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]	"AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5." Bonsegna S., Slocombe S.P., De Bellis L., Baker A. Arch. Biochem. Biophys. 443:74-81(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEX5, TISSUE SPECIFICITY, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF503757 mRNA. Translation: AAM28874.1. AC007478 Genomic DNA. No translation available. CP002688 Genomic DNA. Translation: AED93704.1. AK118614 mRNA. Translation: BAC43213.1. Different initiation.
IPI	IPI00520248.
RefSeq	NP_198112.2. NM_122642.4.
UniGene	At.20193.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q8LKS5.
SMR	Q8LKS5. Positions 75-693.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8LKS5. 1 interaction.
STRING	3702.AT5G27600.1-P.
Proteomic databases
PaxDb	Q8LKS5.
PRIDE	Q8LKS5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G27600.1; AT5G27600.1; AT5G27600.
GeneID	832820.
KEGG	ath:AT5G27600.
Organism-specific databases
TAIR	At5g27600.
Phylogenomic databases
eggNOG	COG1022.
HOGENOM	HOG000159459.
InParanoid	Q8LKS5.
KO	K01897.
OMA	DVMDFLR.
PhylomeDB	Q8LKS5.
Enzyme and pathway databases
BioCyc	MetaCyc:AT5G27600-MONOMER.
UniPathway	UPA00199.
Gene expression databases
Genevestigator	Q8LKS5.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. 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

LACS7_ARATH

Accession

Primary (citable) accession number: Q8LKS5
Secondary accession number(s): Q8GWV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 30, 2010
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program