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InterPro: IPR013751 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III

Protein matchesHelp
UniProtKB
Matches:
2684 proteins
AccessionHelp IPR013751 ACP_syn_III
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR004655 Beta-ketoacyl-acyl carrier protein synthase III (FabH)
IPR016038 Thiolase-like, subgroup
IPR016039 Thiolase-like
IPR017236 Glycine/sarcosine/betaine reductase, component C, beta
GO Term annotationHelp
Process GO:0006633 fatty acid biosynthetic process
Function GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Fatty acid synthesis (FAS) is a vital aspect of cellular physiology which can occur by two distinct pathways. The FAS I pathway, which generally only produces palmitate, is found in eukaryotes and is performed either by a single polypeptide which contains all the reaction centres needed to form a fatty acid, or by two polypeptides which interact to form a multifunctional complex. The FAS II pathway, which is capable of producing many different fatty acids, is found in mitochondria, bacteria, plants and parasites, and is performed by many distinct proteins, each of which catalyses a single step within the pathway. The large diversity of products generated by this pathway is possible because the acyl carrier protein (ACP) intermediates are diffusible entities that can be diverted into other biosynthetic pathways [1].

3-Oxoacyl-[acyl carrier protein (ACP)] synthase III catalyses the first condensation step within the FAS II pathway, using acetyl-CoA as the primer and malonyl-ACP as the acceptor, as shown below.

Acyl-[ACP] + malonyl-[ACP] = 3-oxoacyl-[ACP] + CO(2) + [ACP]

The oxoacyl-ACP formed by this reaction subsequently enters the elongation cycle, where the acyl chain is progressively lengthened by the combined activities of several enzymes.

The enzymes studied so far are homodimers, where each monomer consists of two domains (N-terminal and C-terminal) which are similar in structure, but not in sequence [2, 3]. This entry represents a conserved region within the N-terminal domain.

Structural linksHelp
SCOP: c.95.1.2
CATH: 3.40.47.10
Database linksHelp
Enzyme: EC:2.3.1
Pfam Clan: CL0046.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013751 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A5TZR3 3-oxoacyl-[acyl-carrier-protein] synthase 3

O30256 UPF0219 protein AF_2415

P31176 3-oxoacyl-[acyl-carrier-protein] synthase 3

P49243 3-oxoacyl-[acyl-carrier-protein] synthase III, chloroplastic

P73951 3-oxoacyl-[acyl-carrier-protein] synthase 3

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004656 Putative condensing enzyme FabH-related
IPR004655 Beta-ketoacyl-acyl carrier protein synthase III (FabH)
IPR013747 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C-terminal
IPR016039 Thiolase-like
IPR016038 Thiolase-like, subgroup
IPR013751 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. White SW, Zheng J, Zhang YM, Rock .
The structural biology of type II fatty acid biosynthesis.
Annu. Rev. Biochem. 74 791-831 2005 [PubMed: 15952903]
http://dx.doi.org/10.1146/annurev.biochem.74.082803.133524
2. Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK.
Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
J. Mol. Biol. 307 341-56 2001 [PubMed: 11243824]
http://dx.doi.org/10.1006/jmbi.2000.4457
3. Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM.
Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.
Structure 10 1559-68 2002 [PubMed: 12429097]
http://dx.doi.org/10.1016/S0969-2126(02)00889-4

Additional ReadingHelp
Alhamadsheh MM, Musayev F, Komissarov AA, Sachdeva S, Wright HT, Scarsdale N, Florova G, Reynolds KA.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes.
Chem. Biol. 14 2007 513-24 [PubMed: 17524982]
http://dx.doi.org/10.1016/j.chembiol.2007.03.013
Musayev F, Sachdeva S, Scarsdale JN, Reynolds KA, Wright HT.
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.
J. Mol. Biol. 346 2005 1313-21 [PubMed: 15713483]
http://dx.doi.org/10.1016/j.jmb.2004.12.044
Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT, Khandekar SS.
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
Protein Sci. 14 2005 2087-94 [PubMed: 15987898]
http://dx.doi.org/10.1110/ps.051501605
Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H, Reynolds KA.
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
Bioorg. Chem. 36 2008 85-90 [PubMed: 18096200]
http://dx.doi.org/10.1016/j.bioorg.2007.11.001
Sachdeva S, Musayev FN, Alhamadsheh MM, Scarsdale JN, Wright HT, Reynolds KA.
Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.
Chem. Biol. 15 2008 402-12 [PubMed: 18420147]
http://dx.doi.org/10.1016/j.chembiol.2008.03.007
Abbadi A, Brummel M, Schutt BS, Slabaugh MB, Schuch R, Spener F.
Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.
Biochem. J. 345 Pt 1 2000 153-60 [PubMed: 10600651]
http://dx.doi.org/10.1042/0264-6021:3450153
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InterPro 23.1