Protein Family Models

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

Gene:

menI

Date:

2021-05-27

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate| MaoC family dehydratase similar to Arabidopsis thaliana peroxisomal enoyl-CoA hydratase 2, which catalyzes a hydration step in peroxisomal beta-oxidation

Date:

2017-03-02

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