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glnA glnA asnB asnB hisH hisH pyrG pyrG asnH asnH pdxT pdxT pabA pabA glmS glmS glsA glsA guaA guaA purQ purQ purF purF asnO asnO carA carA carB carB glsB glsB pyrAA pyrAA pyrAB pyrAB gltA gltA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
glnAGlutamine synthetase; Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA- binding active state and turns on the transcription of genes required for nitrogen assimilation. Under condi [...] (444 aa)
asnBAsparagine synthetase; Main asparagine synthetase in vegetative cells. (632 aa)
hisHAmidotransferase (glutaminase); 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 (By similarity). (212 aa)
pyrGCTP synthetase; 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. (535 aa)
asnHAsparagine synthetase (glutamine-hydrolyzing); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparagine synthetase family. (747 aa)
pdxTGlutamine amidotransferase for pyridoxal phosphate synthesis; 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. (196 aa)
pabA4-amino-4-deoxychorismate synthase; Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Also involved in the biosynthesis of anthranilate. (194 aa)
glmSL-glutamine-D-fructose-6-phosphate amidotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (600 aa)
glsAGlutaminase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (327 aa)
guaAGMP synthetase; Catalyzes the synthesis of GMP from XMP. (513 aa)
purQPhosphoribosylformylglycinamidine synthetase 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 [...] (227 aa)
purFGlutamine phosphoribosylpyrophosphate amidotransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (476 aa)
asnOAsparagine synthetase; Asparagine synthetase involved in sporulation. (614 aa)
carAArginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (353 aa)
carBArginine-specific carbamoyl-phosphate synthetase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CarB family. (1030 aa)
glsBGlutaminase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (309 aa)
pyrAAPyrimidine-specific carbamoyl-phosphate synthetase (small subunit, glutaminase subunit); Evidence 2b: Function of strongly homologous gene; enzyme. (364 aa)
pyrABPyrimidine-specific carbamoyl-phosphate synthetase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CarB family. (1071 aa)
gltAGlutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. (1520 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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