Protein Family Models

This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important. (from Pfam)

Date:

2024-08-14

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

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

Date:

2024-05-09

TIGR00369 describes a set of hotdog fold thioesterases, found either as stand-alone protein or as a domain of a multifunctional protein. Examples include EntH (the proofreading thioesterase of enterobactin biosynthesis), MenI (1,4-dihydroxy-2-naphthoyl-CoA hydrolase), and PaaI (hydroxyphenylacetyl-CoA thioesterase).

Date:

2021-10-26