Protein Family Models

This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily [1]. [1]. 15307895. The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. Dillon SC, Bateman A;. BMC Bioinformatics 2004;5:109-109. (from Pfam)

Date:

2024-10-16

This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyse the hydrolysis of other long chain fatty acyl-CoA thioesters. [1]. 9837940. The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3. Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D, Holden HM;. J Biol Chem 1998;273:33572-33579. [2]. 8805534. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL;. Structure 1996;4:253-264. (from Pfam)

Date:

2024-10-16

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 [1]. These proteins are usually composed of a pair of tandem HotDog domains. This entry represents the N-terminal one of the pair. [1]. 7479856. Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering. Yuan L, Voelker TA, Hawkins DJ;. Proc Natl Acad Sci U S A 1995;92:10639-10643. [2]. 1621095. Fatty acid biosynthesis redirected to medium chains in transgenic oilseed plants. Voelker TA, Worrell AC, Anderson L, Bleibaum J, Fan C, Hawkins DJ, Radke SE, Davies HM;. Science 1992;257:72-74. [3]. 15531590. 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. Mayer KM, Shanklin J;. J Biol Chem 2004; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

tol-pal system-associated acyl-CoA thioesterase YbgC catalyzes the hydrolysis of short chain aliphatic acyl-CoA thioesters

Date:

2022-10-06

The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism).

Gene:

ybgC

Date:

2024-06-14

This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon.

Date:

2021-05-12