arath-AT5G20060

 
Arabidopsis thaliana (Mouse-ear cress) Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress) putative lysophospholipase (hypothetical protein)

Comment
Burger et al. show that Acyl-protein thioesterase structures present a long tunnel for accommodation of long-chain fatty acids and release the product by use of a flexible loop tunnel lid. Homologous deacetylases use a hydrophobic residue to fix the lid and another residue to close the tunnel entrance. This causes loop rigidity changing the catalytic preference to deacetylation. ZmB6T1C9 as its paralogue in Arabidopsis At5G20060 is an acylprotein thioesterase and not an protein deacetylase


Relationship
Block X
Arabidopsis thaliana position in NCBI Life Tree :
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain.
> cellular organisms: N E > Eukaryota: N E > Viridiplantae: N E > Streptophyta: N E > Streptophytina: N E > Embryophyta: N E > Tracheophyta: N E > Euphyllophyta: N E > Spermatophyta: N E > Magnoliophyta: N E > Mesangiospermae: N E > eudicotyledons: N E > Gunneridae: N E > Pentapetalae: N E > rosids: N E > malvids: N E > Brassicales: N E > Brassicaceae: N E > Camelineae: N E > Arabidopsis: N E > Arabidopsis thaliana: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
No structure
No kinetic



3 Genbank : AY088171, BT000428, BT001175
>3 UniProt links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 UniProtTrembl links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 Interpro links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 Prodom links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 Pfam links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 PIRSF links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 SUPERFAM links 2 more: Q8L9X1, D7LZE7, D7L6W1
>3 QuickSwissBlast links 2 more: Q8L9X1, D7LZE7, D7L6W1
1 Tair database : AT5G20060
 
Sequence
Graphical view for this peptide sequence: arath-AT5G20060
Colored MSA for LYsophospholipase_carboxylesterase (raw)
MSISGAAVGSGRNLRRAVEFGKTHVVRPKGKHQATIVWLHGLGDNGSSWS
QLLETLPLPNIKWICPTAPSQPISLFGGFPSTAWFDVVDINEDGPDDMEG
LDVAAAHVANLLSNEPADIKLGVGGFSMGAATSLYSATCFALGKYGNGNP
YPINLSAIIGLSGWLPCAKTLAGKLEEEQIKNRAASLPIVVCHGKADDVV
PFKFGEKSSQALLSNGFKKVTFKPYSALGHHTIPQELDELCAWLTSTLSL
EG
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MSISGAAVGSGRNLRRAVEFGKTHVVRPKGKHQATIVWLHGLGDNGSSWS
QLLETLPLPNIKWICPTAPSQPISLFGGFPSTAWFDVVDINEDGPDDMEG
LDVAAAHVANLLSNEPADIKLGVGGFSMGAATSLYSATCFALGKYGNGNP
YPINLSAIIGLSGWLPCAKTLAGKLEEEQIKNRAASLPIVVCHGKADDVV
PFKFGEKSSQALLSNGFKKVTFKPYSALGHHTIPQELDELCAWLTSTLSL
EG

no DNA




References
2 more
    Title: A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors
    Burger M, Willige BC, Chory J
    Ref: Nat Commun, 8:2201, 2017 : PubMed

            

    Title: Features of Arabidopsis genes and genome discovered using full-length cDNAs
    Alexandrov NN, Troukhan ME, Brover VV, Tatarinova T, Flavell RB, Feldmann KA
    Ref: Plant Mol Biol, 60:69, 2006 : PubMed

            

    Title: Full-length messenger RNA sequences greatly improve genome annotation
    Haas BJ, Volfovsky N, Town CD, Troukhan M, Alexandrov N, Feldmann KA, Flavell RB, White O, Salzberg SL
    Ref: Genome Biol, 3:RESEARCH0029, 2002 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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