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nadE nadE pyrG pyrG glsA glsA pdxT pdxT hisH hisH purQ purQ
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second shell of interactors
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Your Input:
nadENAD synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (276 aa)
pyrGCTP 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. (534 aa)
glsAGlutaminase; Belongs to the glutaminase family. (306 aa)
pdxTPredicted glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (195 aa)
hisHGlutamine amidotransferase; 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. (206 aa)
purQPhosphoribosylformylglycinamidine synthase, glutamine amidotransferase domain; 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 an [...] (227 aa)
Your Current Organism:
Solibacillus silvestris
NCBI taxonomy Id: 1002809
Other names: S. silvestris StLB046, Solibacillus silvestris StLB046, Solibacillus silvestris str. StLB046, Solibacillus silvestris strain StLB046
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