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Q8LKS5 (LACS7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Protein existenceEvidence 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 lacs6 and lacs7 double mutant 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PEX5Q9FMA34EBI-993851,EBI-993861

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700Long chain acyl-CoA synthetase 7, peroxisomal
PRO_0000401416

Regions

Nucleotide binding266 – 27712ATP Potential
Region526 – 55025Fatty acid-binding Potential
Motif10 – 189Microbody targeting signal Potential
Motif698 – 7003Microbody targeting signal Potential

Experimental info

Sequence conflict6571F → L in AAM28874. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8LKS5 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: EAD95B9F50DA75DB

FASTA70077,353
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_198112.2. NM_122642.4.
UniGeneAt.20193.

3D structure databases

ProteinModelPortalQ8LKS5.
SMRQ8LKS5. Positions 75-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18094. 1 interaction.
IntActQ8LKS5. 1 interaction.
STRING3702.AT5G27600.1-P.

Proteomic databases

PaxDbQ8LKS5.
PRIDEQ8LKS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G27600.1; AT5G27600.1; AT5G27600.
GeneID832820.
KEGGath:AT5G27600.

Organism-specific databases

TAIRAT5G27600.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
InParanoidQ8LKS5.
KOK01897.
OMAYEELCQN.
PhylomeDBQ8LKS5.

Enzyme and pathway databases

BioCycARA:AT5G27600-MONOMER.
MetaCyc:AT5G27600-MONOMER.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorQ8LKS5.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLACS7_ARATH
AccessionPrimary (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: June 11, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names