Protein Family Models

Anthranilate synthase (EC:4.1.3.27) catalyses the first step in the biosynthesis of tryptophan. Component I catalyses the formation of anthranilate using ammonia and chorismate. The catalytic site lies in the adjacent region, described in the chorismate binding enzyme family (Pfam:PF00425). This region is involved in feedback inhibition by tryptophan [1]. This family also contains a region of Para-aminobenzoate synthase component I (EC 4.1.3.-). [1]. 11371633. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE;. Proc Natl Acad Sci U S A 2001;98:6021-6026. [2]. 11450855. A metabolic node in action: chorismate-utilizing enzymes in microorganisms. Dosselaere F, Vanderleyden J;. Crit Rev Microbiol 2001;27:75-131. (from Pfam)

Date:

2025-02-02

This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase. [1]. 11371633. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE;. Proc Natl Acad Sci U S A 2001;98:6021-6026. [2]. 11450855. A metabolic node in action: chorismate-utilizing enzymes in microorganisms. Dosselaere F, Vanderleyden J;. Crit Rev Microbiol 2001;27:75-131. (from Pfam)

Date:

2025-02-01

This enzyme resembles some other chorismate-binding enzymes, including para-aminobenzoate synthase (pabB) and isochorismate synthase. There is a fairly deep split between two sets, seen in the pattern of gaps as well as in amino acid sequence differences. Archaeal enzymes have been excluded from this model (and are now found in TIGR01820) as have a clade of enzymes which constitute a TrpE paralog which may have PabB activity (TIGR01824). This allows the B. subtilus paralog which has been shown to have PabB activity to score below trusted to this model. This model contains sequences from gram-positive bacteria, certain proteobacteria, cyanobacteria, plants, fungi and assorted other bacteria. A second family of TrpE enzymes is modelled by TIGR00565. The breaking of the TrpE family into these diverse models allows for the separation of the models for the related enzyme, PabB.

Gene:

trpE

Date:

2021-04-27