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Family Report for: Thioesterase


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Thioesterase domains often occur integrated in or associated with peptide synthetases which are involved in the non-ribosomal synthesis of peptide antibiotics. Thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Only the last domain TE thioesterase of the acv synthetase (acvs) is included in ESTHER (Polyketide synthase Polyene PKS). Human fatty acid synthase (FAS) is uniquely expressed at high levels in many tumor types. Pharmacological inhibition of FAS therefore represents an important therapeutic opportunity. The drug Orlistat, which has been approved by the US Food and Drug Administration, inhibits FAS, induces tumor cell-specific apoptosis. Families TE-16 TE-17 TE-18 in ThYme database

Interpro : IPR001031 (Thioesterase), IPR012223 (Thioesterase type II, NRPS/PKS/S-FAS TEII), IPR023102 (Fatty acid synthase, domain 2 Fatty_acid_synthase_dom_2), IPR011412 (Coronamic acid biosynthesis thioesterase CmaT), IPR020802 (Polyketide synthase, thioesterase domain), IPR012367 (Uncharacterised conserved protein thioesterase UCP_Testerase)
Pdoc :
PFam : PF00975 (Thioesterase)
Prints :
Prosite :
no EC number

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin : Text only/graphic display
Seed alignment with MAFFT : No colour/coloured with Mview
Alignment with MAFFT : No colour/coloured with Mview
Dendrogram : Graphical display, obtained with the dnd file produced by Clustalw
HMM profile : HMM profile

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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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