Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9T009

- LACS5_ARATH

UniProt

Q9T009 - LACS5_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Long chain acyl-CoA synthetase 5

Gene

LACS5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Pathwayi

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. 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.
ReactomeiREACT_235205. Synthesis of very long-chain fatty acyl-CoAs.
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: 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.

Expressioni

Gene expression databases

GenevestigatoriQ9T009.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G11030.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9T009.
SMRiQ9T009. Positions 82-574.
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.
OMAiMLGHREI.
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 .
PIRi T01875.
T04298.
T08182.
RefSeqi NP_192841.1. NM_117173.1.
UniGenei At.33591.

3D structure databases

ProteinModelPortali Q9T009.
SMRi Q9T009. Positions 82-574.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G11030.1-P.

Proteomic databases

PaxDbi Q9T009.
PRIDEi Q9T009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G11030.1 ; AT4G11030.1 ; AT4G11030 .
GeneIDi 826704.
KEGGi ath:AT4G11030.

Organism-specific databases

TAIRi AT4G11030.

Phylogenomic databases

eggNOGi COG1022.
HOGENOMi HOG000159459.
InParanoidi Q9T009.
KOi K01897.
OMAi MLGHREI.
PhylomeDBi Q9T009.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci ARA:AT4G11030-MONOMER.
MetaCyc:AT4G11030-MONOMER.
Reactomei REACT_235205. Synthesis of very long-chain fatty acyl-CoAs.

Gene expression databases

Genevestigatori Q9T009.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 82 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