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Q9T009

- LACS5_ARATH

UniProt

Q9T009 - LACS5_ARATH

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
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Magnesium.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

    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: 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 82-583.
    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.
    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

    MTSQKRFIFE VEAAKEATDG NPSVGPVYRS TFAQNGFPNP IDGIQSCWDI    50
    FRTAVEKYPN NRMLGRREIS NGKAGKYVWK TYKEVYDIVI KLGNSLRSCG 100
    IKEGEKCGIY GINCCEWIIS MEACNAHGLY CVPLYDTLGA GAVEFIISHA 150
    EVSIAFVEEK KIPELFKTCP NSTKYMKTVV SFGGVKPEQK EEAEKLGLVI 200
    HSWDEFLKLG EGKQYELPIK KPSDICTIMY TSGTTGDPKG VMISNESIVT 250
    ITTGVMHFLG NVNASLSEKD VYISYLPLAH VFDRAIEECI IQVGGSIGFW 300
    RGDVKLLIED LGELKPSIFC AVPRVLDRVY TGLQQKLSGG GFFKKKVFDV 350
    AFSYKFGNMK KGQSHVAASP FCDKLVFNKV KQGLGGNVRI ILSGAAPLAS 400
    HIESFLRVVA CCNVLQGYGL TESCAGTFAT FPDELDMLGT VGPPVPNVDI 450
    RLESVPEMNY DALGSTPRGE ICIRGKTLFS GYYKREDLTK EVFIDGWLHT 500
    GDVGEWQPNG SMKIIDRKKN IFKLAQGEYV AVENLENVYS QVEVIESIWV 550
    YGNSFESFLV AIANPAQQTL ERWAVENGVN GDFNSICQNA KAKAFILGEL 600
    VKTAKENKLK GFEIIKDVHL EPVAFDMERD LLTPTYKKKR PQLLKYYQNV 650
    IHEMYKTTKE SLASGQ 666
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 82-583.
    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.

    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

    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: October 1, 2014
    This is version 81 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