Summary: Acyl-ACP thioesterase
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Acyl-ACP thioesterase Provide feedback
This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid .
Yuan L, Voelker TA, Hawkins DJ; , Proc Natl Acad Sci U S A 1995;92:10639-10643.: Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering. PUBMED:7479856 EPMC:7479856
Voelker TA, Worrell AC, Anderson L, Bleibaum J, Fan C, Hawkins DJ, Radke SE, Davies HM; , Science 1992;257:72-74.: Fatty acid biosynthesis redirected to medium chains in transgenic oilseed plants. PUBMED:1621095 EPMC:1621095
Mayer KM, Shanklin J; , J Biol Chem 2004; [Epub ahead of print]: A structural model of the plant acyl-acyl carrier protein thioesterase FatB comprised of two helix/4-stranded sheet domains: The N-terminal domain containing residues that affect specificity, the C-terminal domain containing catalytic residues. PUBMED:15531590 EPMC:15531590
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002864
This entry represents various acyl-acyl carrier protein (ACP) thioesterases (TE) which terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid [PUBMED:7479856]. These proteins contain a duplication of two 4HBT-like domains.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||thiolester hydrolase activity (GO:0016790)|
|Biological process||fatty acid biosynthetic process (GO:0006633)|
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The HotDog fold was first observed in the structure of Escherichia coli beta-hydroxydecanoyl thiol ester dehydratase (FabA), where Leesong et al. noticed that each subunit of this dimeric enzyme contained a mixed alpha + beta 'hot dog' fold. They described the seven-stranded antiparallel beta-sheet as the 'bun', which wraps around a five-turn alpha-helical 'sausage', This superfamily contains a diverse range of enzymes. Membership includes numerous prokaryotic, archaeal and eukaryotic proteins involved in several related, but distinct, catalytic activities, from metabolic roles such as thioester hydrolysis in fatty acid metabolism, to degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. The superfamily also includes FapR, a non-catalytic bacterial homologue that is involved in transcriptional regulation of fatty acid biosynthesis .
The clan contains the following 13 members:4HBT 4HBT_2 4HBT_3 Acyl-ACP_TE Acyl_CoA_thio AfsA DUF4442 FabA FcoT MaoC_dehydrat_N MaoC_dehydratas PS-DH YiiD_Cterm
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Curation and family details
|Seed source:||Pfam-B_928 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||27|
|Number in full:||1578|
|Average length of the domain:||228.20 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||89.64 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Acyl-ACP_TE domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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