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InterPro: IPR002864 Acyl-ACP thioesterase

Protein matchesHelp
UniProtKB
Matches:
591 proteins
AccessionHelp IPR002864 Acyl-ACP_TE
TypeHelp Family
SignaturesHelp
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) which terminate fatty acyl group extension via hydrolyzing an acyl group on a fatty acid [1].

Structural linksHelp
SCOP: d.38.1.8
CATH: 3.10.129.10
Database linksHelp
Enzyme: EC:3.1.2
PANDIT: PF01643
Blocks: IPB002864
Pfam Clan: CL0050.8

Taxonomic coverageHelp

Example proteinsHelp
Q10856 Uncharacterized protein Rv2001/MT2057

Q39473 Myristoyl-acyl carrier protein thioesterase, chloroplastic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002864 Acyl-ACP thioesterase
SWISS-MODEL
ModBase

PublicationsHelp
1. Yuan L, Voelker TA, Hawkins DJ.
Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering.
Proc. Natl. Acad. Sci. U.S.A. 92 10639-43 1995 [PubMed: 7479856]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=7479856

Additional ReadingHelp
Voelker TA, Worrell AC, Anderson L, Bleibaum J, Fan C, Hawkins DJ, Radke SE, Davies HM.
Fatty acid biosynthesis redirected to medium chains in transgenic oilseed plants.
Science 257 1992 72-4 [PubMed: 1621095]
http://www.sciencemag.org/cgi/content/abstract/257/5066/72
Mayer KM, Shanklin J.
A structural model of the plant acyl-acyl carrier protein thioesterase FatB comprises two helix/4-stranded sheet domains, the N-terminal domain containing residues that affect specificity and the C-terminal domain containing catalytic residues.
J. Biol. Chem. 280 2005 3621-7 [PubMed: 15531590]
http://dx.doi.org/10.1074/jbc.M411351200
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InterPro 23.1