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Links from Protein

Items: 5

1.

hotdog domain-containing protein

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
Family Accession:
NF015048.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

acyl-CoA thioesterase

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

Date:
2024-04-30
Family Accession:
10787832
Method:
Sparcle
5.

hotdog fold thioesterase

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).

GO Terms:
Molecular Function:
thiolester hydrolase activity (GO:0016790)
Date:
2021-10-26
Family Accession:
TIGR00369.1
Method:
HMM
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