Summary: 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal
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3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal Provide feedback
This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:184.108.40.206, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Abbadi A, Brummel M, Schutt BS, Slabaugh MB, Schuch R, Spener F; , Biochem J 2000;345:153-160.: Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme. PUBMED:10600651 EPMC:10600651
Internal database links
|Similarity to PfamA using HHSearch:||Chal_sti_synt_C Thiolase_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013747
This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)|
|Biological process||lipid biosynthetic process (GO:0008610)|
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Thiolases are ubiquitous and form a large superfamily. Thiolases can function either degradatively, in the beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic thiolases catalyse the formation of acetoacetyl-CoA from two molecules of acetyl-CoA . This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in a wide range of biosynthetic pathways . Thiolase are usually dimeric or tetrameric enzymes. Within each monomer there are two similar domains related by pseudo dyad. The N-terminal of these two domains contains a large insertion of about 100 amino acids.
The clan contains the following 13 members:ACP_syn_III ACP_syn_III_C Chal_sti_synt_C Chal_sti_synt_N FAE1_CUT1_RppA HMG_CoA_synt_C HMG_CoA_synt_N ketoacyl-synt Ketoacyl-synt_2 Ketoacyl-synt_C SpoVAD Thiolase_C Thiolase_N
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Curation and family details
|Seed source:||Pfam-B_67 (release 18.0)|
|Number in seed:||187|
|Number in full:||7398|
|Average length of the domain:||89.30 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||25.98 %|
|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:||5|
|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 ACP_syn_III_C domain has been found. There are 91 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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