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JT27_04355 protein (Alcaligenes faecalis) - STRING interaction network
"JT27_04355" - Glutamate synthase in Alcaligenes faecalis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
JT27_04355Glutamate synthase; Derived by automated computational analysis using gene prediction method- Protein Homology (1577 aa)    
Predicted Functional Partners:
gltD
Glutamate synthase is composed of subunits alpha and beta; beta subunit is a flavin adenine dinucleotide-NADPH dependent oxidoreductase; provides electrons to the alpha subunit, which binds L-glutamine and 2-oxoglutarate and forms L-glutamate; Derived by automated computational analysis using gene prediction method- Protein Homology (490 aa)
  0.999
JT27_15075
Converts 2-oxoglutarate to glutamate; in Escherichia coli this enzyme plays a role in glutamate synthesis when the cell is under energy restriction; uses NADPH; forms a homohexamer; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family (446 aa)
   
  0.985
JT27_03150
Glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family (429 aa)
   
  0.985
glnA
Forms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method- Protein Homology (470 aa)
   
 
  0.982
glmS
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source (608 aa)
   
  0.952
carB
Carbamoyl-phosphate synthase large chain; Four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity; Derived by automated computational analysis using gene prediction method- Protein Homology (1080 aa)
   
 
  0.950
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family (494 aa)
   
 
  0.946
carA
Carbamoyl-phosphate synthase small chain; Catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers; Derived by automated computational analysis using gene prediction method- Protein Homology (387 aa)
   
 
    0.938
gltA
Citrate synthase; Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the citrate [...] (434 aa)
   
 
  0.929
JT27_14900
Isocitrate dehydrogenase [NADP]; Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (418 aa)
       
  0.919
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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