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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
putC1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source (515 aa)    
Predicted Functional Partners:
putB
Proline dehydrogenase 2; Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source
 0.998
putM
Proline dehydrogenase 1; Converts proline to delta-1-pyrroline-5-carboxylate
 0.989
rocD
Ornithine--oxo-acid transaminase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism
 
 0.965
rocG
Catabolic nad-specific glutamate dehydrogenase rocg; 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 c [...]
 
 0.948
gudB
Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 [...]
 
 0.944
gltA
Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family
  
 
 0.938
proH
Pyrroline-5-carboxylate reductase 1; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline
     
 0.927
dat
D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...]
   
 0.926
proI
Pyrroline-5-carboxylate reductase 2; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline
 
   
 0.925
proG
Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline
     
 0.924
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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