STRINGSTRING
ald ald argG argG purB purB purL/purQ purL/purQ purF purF glmS glmS nadB1 nadB1 gabT gabT carB carB carA carA gltD gltD gltB gltB argH argH got got gab gab CBL57095.1 CBL57095.1 glnA glnA aspA1 aspA1 aspA2 aspA2 pyrB pyrB gdh gdh ansA ansA asnB asnB purA purA nadB2 nadB2 CBL57694.1 CBL57694.1 gadB gadB
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
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
Edges:
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:
aldL-alanine + H2O + NAD+ = pyruvate + NH3 + NADH; Belongs to the AlaDH/PNT family. (371 aa)
argGArgininosuccinate synthase; ATP + L-Citrulline + L-Aspartate <=> AMP + Pyrophosphate + N-(L-Arginino)succinate; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (478 aa)
purBAdenylosuccinate lyase; N6-(1,2-Dicarboxyethyl)-AMP <=> Fumarate + AMP 1-(5prime-Phosphoribosyl)-5-amino-4-(N- succinocarboxamide)-imidazole These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. (477 aa)
purL/purQPhosphoribosylformylglycinamidine synthase subunit PurQ; 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 [...] (225 aa)
purFAmidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (513 aa)
glmSGlutamine--fructose-6-phosphate aminotransferase [isomerizing]; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (614 aa)
nadB1L-aspartate oxidase (LASPO) (Quinolinate synthetase B); Catalyzes the oxidation of L-aspartate to iminoaspartate. (560 aa)
gabT4-aminobutyrate aminotransferase; 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde +; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (445 aa)
carBCarbamoyl-phosphate synthase large chain (Carbamoyl-phosphate synthetase ammonia chain); 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate; Binds 3 manganese ions per subunit; Belongs to the CarB family. (1113 aa)
carACarbamoyl-phosphate synthase small chain; The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides; Belongs to the CarA family. (394 aa)
gltDGlutamate synthase small subunit; 2 L-Glutamate + NADP+ <=> L-Glutamine + 2-Oxoglutarate + NADPH + H+. (489 aa)
gltBGlutamate synthase large subunit (Ferredoxin); 2 L-Glutamate + 2 Oxidized ferredoxin <=> L-Glutamine + 2-Oxoglutarate + 2 Reduced ferredoxin. (1502 aa)
argHArgininosuccinate lyase (Arginosuccinase); N-(L-Arginino)succinate <=> Fumarate + L-Arginine. (452 aa)
gotAspartate aminotransferase. (404 aa)
gabAldehyde dehydrogenase (Succinate-semialdehyde dehydrogenase) (NAD-dependent aldehyde dehydrogenase); Belongs to the aldehyde dehydrogenase family. (488 aa)
CBL57095.1Glutamine synthetase; Glutamate metabolism : ATP + L-Glutamate + NH3 <=> ADP + Orthophosphate + L-Glutamine, Peptidoglycan biosynthesis. (479 aa)
glnAGlutamine synthetase; # ATP + L-Glutamate + NH3 <=> ADP + Orthophosphate + L-Glutamine; Belongs to the glutamine synthetase family. (444 aa)
aspA1Aspartate ammonia-lyase (Aspartase); L-aspartate = fumarate + NH3. (489 aa)
aspA2L-Aspartate <=> Fumarate + NH3. (490 aa)
pyrBCarbamoyl phosphate + L-Aspartate <=> Orthophosphate + N-Carbamoyl-L-aspartate; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. (348 aa)
gdhGlutamate dehydrogenase (NAD(P)-glutamate dehydrogenase); L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH. Homohexamer (By similarity). Belongs to the Glu/Leu/Phe/Val dehydrogenases family. Evidenced as a heat stress proetin in P. freudenreichii. (454 aa)
ansAL-asparagine + H2O = L-aspartate + NH3. (356 aa)
asnBAsparagine synthase (Glutamine-hydrolyzing); ATP + L-Aspartate + L-Glutamine + H2O <=> AMP + Pyrophosphate + L-Asparagine + L-Glutamate. (636 aa)
purAAdenylosuccinate synthetase (IMP--aspartate ligase) (AdSS) (AMPSase); Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. (427 aa)
nadB2L-aspartate oxidase (LASPO) (Quinolinate synthetase B). (529 aa)
CBL57694.1Aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (444 aa)
gadBL-Glutamate <=> 4-Aminobutanoate + CO2 L-Aspartate <=> beta-Alanine + CO2; Belongs to the group II decarboxylase family. (470 aa)
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.