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Q9SJD4 (LACS8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Long chain acyl-CoA synthetase 8

EC=6.2.1.3
Gene names
Name:LACS8
Ordered Locus Names:At2g04350
ORF Names:T1O3, T23O15.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length720 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 and linoleate.

Catalytic activity

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1

Cofactor

Magnesium By similarity.

Pathway

Lipid metabolism; fatty acid metabolism.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Long chain acyl-CoA synthetase 8
PRO_0000401417

Regions

Nucleotide binding279 – 29012ATP Potential
Region554 – 58229Fatty acid-binding Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Experimental info

Sequence conflict256 – 2638EVEKLGQK → DFFKLPPH in AAK96568. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9SJD4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 96ED3FD23AD2ED75

FASTA72078,343
        10         20         30         40         50         60 
MEDSGVNPMD SPSKGSDFGV YGIIGGGIVA LLVPVLLSVV LNGTKKGKKR GVPIKVGGEE 

        70         80         90        100        110        120 
GYTMRHARAP ELVDVPWEGA ATMPALFEQS CKKYSKDRLL GTREFIDKEF ITASDGRKFE 

       130        140        150        160        170        180 
KLHLGEYKWQ SYGEVFERVC NFASGLVNVG HNVDDRVAIF SDTRAEWFIA FQGCFRQSIT 

       190        200        210        220        230        240 
VVTIYASLGE EALIYSLNET RVSTLICDSK QLKKLSAIQS SLKTVKNIIY IEEDGVDVAS 

       250        260        270        280        290        300 
SDVNSMGDIT VSSISEVEKL GQKNAVQPIL PSKNGVAVIM FTSGSTGLPK GVMITHGNLV 

       310        320        330        340        350        360 
ATAAGVMKVV PKLDKNDTYI AYLPLAHVFE LEAEIVVFTS GSAIGYGSAM TLTDTSNKVK 

       370        380        390        400        410        420 
KGTKGDVSAL KPTIMTAVPA ILDRVREGVL KKVEEKGGMA KTLFDFAYKR RLAAVDGSWF 

       430        440        450        460        470        480 
GAWGLEKMLW DALVFKKIRA VLGGHIRFML VGGAPLSPDS QRFINICMGS PIGQGYGLTE 

       490        500        510        520        530        540 
TCAGATFSEW DDPAVGRVGP PLPCGYVKLV SWEEGGYRIS DKPMPRGEIV VGGNSVTAGY 

       550        560        570        580        590        600 
FNNQEKTDEV YKVDEKGTRW FYTGDIGRFH PDGCLEVIDR KKDIVKLQHG EYVSLGKVEA 

       610        620        630        640        650        660 
ALGSSNYVDN IMVHADPINS YCVALVVPSR GALEKWAEEA GVKHSEFAEL CEKGEAVKEV 

       670        680        690        700        710        720 
QQSLTKAGKA AKLEKFELPA KIKLLSEPWT PESGLVTAAL KIKREQIKSK FKDELSKLYA 

« 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 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(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. expand/collapse author list , 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]"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.
[6]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503758 mRNA. Translation: AAM28875.1.
AC006951 Genomic DNA. Translation: AAD25843.1.
AC007213 Genomic DNA. Translation: AAM15458.1.
CP002685 Genomic DNA. Translation: AEC05822.1.
CP002685 Genomic DNA. Translation: AEC05823.1.
AY052664 mRNA. Translation: AAK96568.1.
BT002288 mRNA. Translation: AAN72299.1.
PIRE84456.
RefSeqNP_178516.1. NM_126468.3.
NP_849934.1. NM_179603.2.
UniGeneAt.21686.

3D structure databases

ProteinModelPortalQ9SJD4.
SMRQ9SJD4. Positions 116-711.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G04350.1-P.

Proteomic databases

PaxDbQ9SJD4.
PRIDEQ9SJD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G04350.1; AT2G04350.1; AT2G04350.
AT2G04350.2; AT2G04350.2; AT2G04350.
GeneID814974.
KEGGath:AT2G04350.

Organism-specific databases

TAIRAT2G04350.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
InParanoidQ9SJD4.
KOK01897.
OMAGINDKVN.
PhylomeDBQ9SJD4.
ProtClustDBPLN02387.

Enzyme and pathway databases

BioCycARA:AT2G04350-MONOMER.
ARA:GQT-1997-MONOMER.
MetaCyc:AT2G04350-MONOMER.
SABIO-RKQ9SJD4.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorQ9SJD4.

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 nameLACS8_ARATH
AccessionPrimary (citable) accession number: Q9SJD4
Secondary accession number(s): Q940V0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 90 of the entry and version 1 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