Zn-dependent hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.

Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.

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.

Putative threonine dehydratase.

Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.

Pyridoxal-phosphate dependent enzyme; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.

Probable tryptophan synthase (Alpha chain) protein; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.

Hypothetical protein.

NADH dehydrogenase I, chain D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.