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glsA glsA purQ purQ nosA nosA yhdR yhdR argC argC argJ argJ argB argB argD argD argF argF glsB glsB glnA glnA yodQ yodQ aspB aspB gudB gudB argH argH argG argG ureC ureC ureB ureB ureA ureA rocG rocG argI argI
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
glsAGlutaminase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (327 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)
nosANitric-oxide synthase; Catalyzes the production of nitric oxide. Belongs to the NOS family. Bacterial NOS oxygenase subfamily. (363 aa)
yhdRPutative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (393 aa)
argCN-acetylglutamate gamma-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. (345 aa)
argJOrnithine acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. (406 aa)
argBN-acetylglutamate 5-phosphotransferase (acetylglutamate kinase); Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. (258 aa)
argDN-acetylornithine aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (385 aa)
argFOrnithine carbamoyltransferase; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. (319 aa)
glsBGlutaminase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (309 aa)
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)
yodQPutative deacylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (436 aa)
aspBPutative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa)
gudBCryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] (427 aa)
argHArgininosuccinate lyase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (461 aa)
argGArgininosuccinate synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (403 aa)
ureCUrease (alpha subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. (569 aa)
ureBUrease (beta subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease beta subunit family. (124 aa)
ureAUrease (gamma subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease gamma subunit family. (105 aa)
rocGGlutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] (424 aa)
argIArginase; Involved in the catabolism of arginine. Belongs to the arginase family. (296 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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