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Protein

Long chain acyl-CoA synthetase 5

Gene

LACS5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Mg2+By similarity

Pathway: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi228 – 23912ATPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  • fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G11030-MONOMER.
MetaCyc:AT4G11030-MONOMER.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Long chain acyl-CoA synthetase 5 (EC:6.2.1.3)
Gene namesi
Name:LACS5
Ordered Locus Names:At4g11030
ORF Names:F8M12.15, T22B4.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G11030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 666666Long chain acyl-CoA synthetase 5PRO_0000401413Add
BLAST

Proteomic databases

PaxDbiQ9T009.
PRIDEiQ9T009.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G11030.1.

Structurei

3D structure databases

ProteinModelPortaliQ9T009.
SMRiQ9T009. Positions 82-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 51925Fatty acid-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ9T009.
KOiK01897.
OMAiRTDTCTI.
PhylomeDBiQ9T009.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9T009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSQKRFIFE VEAAKEATDG NPSVGPVYRS TFAQNGFPNP IDGIQSCWDI
60 70 80 90 100
FRTAVEKYPN NRMLGRREIS NGKAGKYVWK TYKEVYDIVI KLGNSLRSCG
110 120 130 140 150
IKEGEKCGIY GINCCEWIIS MEACNAHGLY CVPLYDTLGA GAVEFIISHA
160 170 180 190 200
EVSIAFVEEK KIPELFKTCP NSTKYMKTVV SFGGVKPEQK EEAEKLGLVI
210 220 230 240 250
HSWDEFLKLG EGKQYELPIK KPSDICTIMY TSGTTGDPKG VMISNESIVT
260 270 280 290 300
ITTGVMHFLG NVNASLSEKD VYISYLPLAH VFDRAIEECI IQVGGSIGFW
310 320 330 340 350
RGDVKLLIED LGELKPSIFC AVPRVLDRVY TGLQQKLSGG GFFKKKVFDV
360 370 380 390 400
AFSYKFGNMK KGQSHVAASP FCDKLVFNKV KQGLGGNVRI ILSGAAPLAS
410 420 430 440 450
HIESFLRVVA CCNVLQGYGL TESCAGTFAT FPDELDMLGT VGPPVPNVDI
460 470 480 490 500
RLESVPEMNY DALGSTPRGE ICIRGKTLFS GYYKREDLTK EVFIDGWLHT
510 520 530 540 550
GDVGEWQPNG SMKIIDRKKN IFKLAQGEYV AVENLENVYS QVEVIESIWV
560 570 580 590 600
YGNSFESFLV AIANPAQQTL ERWAVENGVN GDFNSICQNA KAKAFILGEL
610 620 630 640 650
VKTAKENKLK GFEIIKDVHL EPVAFDMERD LLTPTYKKKR PQLLKYYQNV
660
IHEMYKTTKE SLASGQ
Length:666
Mass (Da):74,064
Last modified:May 1, 2000 - v1
Checksum:i6928569968215C90
GO

Sequence cautioni

The sequence AAC33962.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti661 – 6611S → T in AAM28872 (PubMed:12177484).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503755 mRNA. Translation: AAM28872.1.
AF080118 Genomic DNA. Translation: AAC33962.1. Sequence problems.
AL049876 Genomic DNA. Translation: CAB43038.1.
AL161518 Genomic DNA. Translation: CAB81204.1.
CP002687 Genomic DNA. Translation: AEE82963.1.
BT046194 mRNA. Translation: ACI49793.1.
PIRiT01875.
T04298.
T08182.
RefSeqiNP_192841.1. NM_117173.1.
UniGeneiAt.33591.

Genome annotation databases

EnsemblPlantsiAT4G11030.1; AT4G11030.1; AT4G11030.
GeneIDi826704.
KEGGiath:AT4G11030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503755 mRNA. Translation: AAM28872.1.
AF080118 Genomic DNA. Translation: AAC33962.1. Sequence problems.
AL049876 Genomic DNA. Translation: CAB43038.1.
AL161518 Genomic DNA. Translation: CAB81204.1.
CP002687 Genomic DNA. Translation: AEE82963.1.
BT046194 mRNA. Translation: ACI49793.1.
PIRiT01875.
T04298.
T08182.
RefSeqiNP_192841.1. NM_117173.1.
UniGeneiAt.33591.

3D structure databases

ProteinModelPortaliQ9T009.
SMRiQ9T009. Positions 82-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G11030.1.

Proteomic databases

PaxDbiQ9T009.
PRIDEiQ9T009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G11030.1; AT4G11030.1; AT4G11030.
GeneIDi826704.
KEGGiath:AT4G11030.

Organism-specific databases

TAIRiAT4G11030.

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ9T009.
KOiK01897.
OMAiRTDTCTI.
PhylomeDBiQ9T009.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciARA:AT4G11030-MONOMER.
MetaCyc:AT4G11030-MONOMER.

Miscellaneous databases

PROiQ9T009.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(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. "Arabidopsis ORF clones."
    De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    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.

Entry informationi

Entry nameiLACS5_ARATH
AccessioniPrimary (citable) accession number: Q9T009
Secondary accession number(s): O81614, Q8LKS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.