Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 29% identity in aa 29 - 287.

Fumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 29% identity in aa 29 - 287.

Fumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.

Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate.

N-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Phosphoribosylformimino-5-aminoimidazole carboxamide ribotideisomerase. (SW:HIS4_SALTY).

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

DNA gyrase, subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB s [...]

Membrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

Membrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

DNA gyrase, subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB s [...]

Fumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 29% identity in aa 29 - 287.

Fumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

Fumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.

Fumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.

Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 29% identity in aa 29 - 287.

Fumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.

Fumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

DNA gyrase, subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB s [...]

Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.

DNA gyrase, subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB s [...]

Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.

N-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Phosphoribosylformimino-5-aminoimidazole carboxamide ribotideisomerase. (SW:HIS4_SALTY).

Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate.

L-lactate dehydrogenase; Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain; Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

LctP transporter; Transports L-lactate across the membrane. Can also transport D-lactate and glycolate. Seems to be driven by a proton motive force (By similarity).

L-lactate dehydrogenase; Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain; Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Pyruvate dehydrogenase/oxidase FAD and thiamine PPi cofactors, cytoplasmic in absence of cofactors; Similar to E. coli pyruvate oxidase (AAC73958.1); Blastp hit to AAC73958.1 (572 aa), 94% identity in aa 1 - 572; Belongs to the TPP enzyme family.