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
proB1Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (261 aa)    
Predicted Functional Partners:
proA2
Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.
 
 0.999
proA1
Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.
 
 0.999
proC1
Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
 
 0.969
proB2
Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
  
  
 
0.919
rocD
Ornithine aminotransferase is involved in the Urea cycle and it is responsible for the fourth step in arginine biosynthesis. It catalyzes the transfer of an amino group from ornithine to a 2-oxo acid, yielding glutamic-5-semi-aldehyde and an L-amino acid; Uses the Pyridoxal phosphate as cofactor linked to a conserved lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
   
 0.916
pruA
1-pyrroline-5-carboxylate dehydrogenase is involved in L-proline degradation. It catalyzes the reaction: 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH. Belongs to the aldehyde dehydrogenase family and uses NAD as cofactor. Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.904
proC2
Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
 
 0.630
CAZ96574.1
Putative membrane protein; Contains a N-terminal transmembrane segment; Possibly localized in the cytoplasmic membrane; Hypothetical protein.
       0.609
gdhA1
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.535
gdhA2
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.535
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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