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AFY79990.1 | Putative amidohydrolase; PFAM: Carbon-nitrogen hydrolase. (270 aa) | ||||
AFY80119.1 | N-acetylmuramoyl-L-alanine amidase; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; N-acetylmuramoyl-L-alanine amidase. (457 aa) | ||||
AFY80219.1 | Putative metal-dependent hydrolase; PFAM: Putative cyclase. (235 aa) | ||||
AFY80718.1 | PFAM: L-asparaginase II. (315 aa) | ||||
AFY81056.1 | Chemotaxis response regulator containing a CheY-like receiver domain and a methylesterase domain; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. (336 aa) | ||||
AFY81956.1 | Hypothetical protein. (230 aa) | ||||
cheB | Chemotaxis response regulator containing a CheY-like receiver domain and a methylesterase domain; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. (400 aa) | ||||
ureC | PFAM: Urease alpha-subunit, N-terminal domain; Amidohydrolase family; TIGRFAM: urease, alpha subunit. (577 aa) | ||||
AFY82800.1 | Deacetylase, histone deacetylase/acetoin utilization protein; PFAM: Histone deacetylase domain. (305 aa) | ||||
AFY82821.1 | PFAM: Penicillin amidase. (679 aa) | ||||
hisH | Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. (214 aa) | ||||
ureB | PFAM: Urease beta subunit; TIGRFAM: urease, beta subunit; Belongs to the urease beta subunit family. (103 aa) | ||||
ureA | PFAM: Urease, gamma subunit; TIGRFAM: urease, gamma subunit; Belongs to the urease gamma subunit family. (100 aa) | ||||
def | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (187 aa) | ||||
AFY83382.1 | PFAM: N-acetylmuramoyl-L-alanine amidase; Bacterial SH3 domain; manually curated. (586 aa) | ||||
pyrG | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (554 aa) | ||||
AFY83410.1 | Deacetylase, histone deacetylase/acetoin utilization protein; PFAM: Histone deacetylase domain. (313 aa) | ||||
AFY83480.1 | PFAM: Localisation of periplasmic protein complexes. (505 aa) | ||||
AFY83683.1 | PFAM: N-acetylmuramoyl-L-alanine amidase; Localisation of periplasmic protein complexes. (595 aa) | ||||
cheB-2 | Chemotaxis response regulator containing a CheY-like receiver domain and a methylesterase domain; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. (348 aa) | ||||
purU | Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (285 aa) | ||||
AFY83772.1 | PFAM: Penicillin amidase. (851 aa) | ||||
nadE | NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (585 aa) | ||||
purQ | Phosphoribosylformylglycinamidine synthase I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist i [...] (233 aa) | ||||
AFY84162.1 | Putative glutamine amidotransferase; PFAM: Peptidase C26. (251 aa) | ||||
AFY84311.1 | TIGRFAM: N-acetylglucosamine-6-phosphate deacetylase. (413 aa) | ||||
AFY84423.1 | PFAM: N-acetylmuramoyl-L-alanine amidase; Localisation of periplasmic protein complexes. (622 aa) | ||||
AFY84424.1 | PFAM: N-acetylmuramoyl-L-alanine amidase; Localisation of periplasmic protein complexes. (617 aa) | ||||
AFY84574.1 | Amidase, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit; PFAM: Amidase; Belongs to the amidase family. (468 aa) | ||||
AFY84734.1 | N-carbamoylputrescine amidase; PFAM: Carbon-nitrogen hydrolase; TIGRFAM: N-carbamoylputrescine amidase. (286 aa) | ||||
lpxC | UDP-3-O-(3-hydroxymyristoyl) N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the LpxC family. (291 aa) | ||||
def-2 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (177 aa) |