STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
gltBCatalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. (1448 aa)    
Predicted Functional Partners:
AIQ98616.1
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
AIR00905.1
(Fe-S)-binding protein; Unknown function; in E. coli the aegA gene is regulated by Fnr, NarXL, and NarQ (but not ArcA), induced under anaerobic conditions and repressed in the presence of nitrate (anaerobic); Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AIR01109.1
Glutamate synthase; Unknown function; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AIR00908.1
Putative selenate reductase subunit YgfK; With YgfM and YgfN forms a selenate reductase, which seems to catalyze the reduction of selenate to selenite; YgfK mutants are unable to reduce selenate; involved in purine salvage process; seems to act as an oxidoreductase, but sequence similarity suggests it is a dihydrothymine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
fadH
NADPH-dependent 2,4-dienoyl-CoA reductase; Catalyzes the formation of trans-2- enoyl-CoA from 2,4-dienoyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.997
AIR01451.1
Glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
  
 0.997
AIR01763.1
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.
  
 0.997
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.
  
 
 0.982
carB
Carbamoyl phosphate synthase large subunit; 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.
  
 
 0.969
glmS
Glutamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
   
 0.956
Your Current Organism:
Pluralibacter gergoviae
NCBI taxonomy Id: 61647
Other names: ATCC 33028, CCUG 14557, CDC 604-77, CIP 76.01, CIP 76.1, DSM 9245, Enterobacter gergoviae, Enterobacter gergoviensis, LMG 5739, LMG:5739, NBRC 105706, NCTC 11434, P. gergoviae
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