TrpA protein; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.

Indole-3-glycerol phosphate synthase (IGPS). catalytic activity:1-(2-carboxyphenylamino)-1-deoxy-d-ribulose 5-phosphate = 1-(indol-3-yl)glycerol 3-phosphate + co(2) + h(2)o. pathway: tryptophan biosynthesis; fourth step. InterPro: Indole-3-glycerol phosphate synthase; High confidence in function and specificity; Belongs to the TrpC family.

Anthranilate synthase component II (Glutamine amido-transferase). catalytic activity: chorismate + l-glutamine = anthranilate + pyruvate + l-glutamate. pathway: tryptophan biosynthesis; first step. TIGRFAM: trpG_papA: glutamine amidotransferase of anthranilate synthase or para-aminobenzoate synthase; High confidence in function and specificity.

1,4-alpha-glucan branching enzyme; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).

Anthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.

Para-aminobenzoate synthase component I (EC 4.1.3.-) (ADC synthase). CATALYZES THE BIOSYNTHESIS OF 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND GLUTAMINE. InterPro: Anthranilate synthase component I and chorismate binding enzyme pabB: para-aminobenzoate synthase component I; Specificity unclear.

Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.

Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.

The glycosyl transferase family includes anthranilate phosphoribosyltransferase (TrpD, EC: 2.4.2.18) and thymidine phosphorylase (EC: 2.4.2.2). All these proteins can transfer a phosphorylated ribose substrate. Similar to sprot|YBIB_ECOLI (40%) and to sprot|TRPD_SULSO (25%). Pfam (PF02885): Glycosyl transferase, family 3; Family membership.